Application: IP, ELISA, WB, FC, IEM

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Human

CD9 is a cell surface glycoprotein which belongs to the tetraspanin superfamily. CD9 is known to complex with integrins and other transmembrane 4 superfamily proteins. It can modulate cell adhesion and migration and also trigger platelet activation and aggregation. Importantly, it is found on the surface of exosomes.

Exosomes are cell-derived vesicles bounded by a lipid bilayer membrane and exhibiting a diameter of 50 to 150 nm. They are secreted from cultured cells and are observed in body fluids such as saliva, blood, urine, amniotic fluid, malignant ascites. Recent studies indicate that exosomes contain various proteins and RNAs, suggesting a role in information transfer between cells.

This monoclonal antibody can be used to immunoprecipitate exosomes from serum and culture supernatants.

References:
1) Shigeyasu Tsuda et al., Scientific Reports volume 7, Article number: 12989 (2017)
2) N Nishida-Aoki et al., Mol Ther. 2017 Jan 4;25(1):181-191. doi: 10.1016/j.ymthe.2016.10.009.
3) Matsuzaki K et al., Oncotarget. 2017 Apr 11; 8(15): 24668–24678. doi: 10.18632/oncotarget.14969
4) Kazutoshi Fujita et al., Sci Rep. 2017; 7: 42961. doi: 10.1038/srep42961
5) Yoshioka Y et al., Nat Commun. 2014 Apr 7;5:3591. doi: 10.1038/ncomms4591.
6) Saito S et al., Sci Rep. 2018 Mar 5;8(1):3997. doi: 10.1038/s41598-018-22450-2.
7) Yagi Y et al., Neurosci Lett. 2017 Jan 1;636:48-57. doi: 10.1016/j.neulet.2016.10.042.
8) Ueda K et al., Sci Rep. 2014 Aug 29;4:6232. doi: 10.1038/srep06232.

Application: IP, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Plant, Tomato, Soybean, Cowpea

Application of the Arabidopsis model system has yielded a regulatory pathway for ionic homeostasis under salt stress. The pathway was discovered through the cloning of the salt overly sensitive (SOS) genes. Mutations in the SOS genes render Arabidopsis plants more sensitive to Na+ stress. The pathway begins with SOS3, a myristoylated protein with three EF hands for calcium binding. SOS3 interacts physically with SOS2, which is a serine/threonine protein kinase. One downstream target of SOS3–SOS2 kinase complex is SOS1, which is a plasma membrane Na+–H+ antiporter that exports Na+ from the cell. SOS1 expression is upregulated by salt stress in wild-type Arabidopsis plants but this upregulation is reduced by sos3 or sos2 mutations. It remains to be seen whether or not SOS3–SOS2 directly regulates the activities of SOS1 and other transporter through phosphorylation. Remaining components in the SOS pathway are expected to be identified by cloning additional SOS genes and screening for second site suppressor and enhancer mutations in the sos mutant backgrounds. [from: Zhu JK. (2001) Plant salt tolerance. TRENDS in Plant Science. 6(2):66-71]

References:
1) Yuasa T, Ishibashi Y. and Iwaya-Inoue M. (2012) A flower specific calcineurin B-like molecule (CBL)-interacting protein kinase (CIPK) homolog in tomato cultivar Micro-Tom (Solanum lycopersicum L.). American Journal of Plant Sciences. 3:753-763.
2) Imamura M, Yuasa T, Takahashi T, Nakamura N, Nang MPSH, Zheng SH, Shimazaki K. and Iwaya-Inoue M. (2008) Isolation and characterization of a cDNA coding cowpea (Vigna unguiculata (L.) Walp.) calcineurin B-like protein interacting protein kinase, VuCIPK1. Plant Biotechnol. 25:437-445.

Application: IP

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Rat, Human

Muscarinic acetylcholine receptors, or mAChRs, are acetylcholine receptors that form G protein-coupled receptor complexes in the cell membranes of certain neurons and other cells. They play several roles, including acting as the main end-receptor stimulated by acetylcholine released from postganglionic fibers in the parasympathetic nervous system. Muscarinic receptors are so named because they are more sensitive to muscarine than to nicotine. By the use of selective radioactively labeled agonist and antagonist substances, five subtypes of muscarinic receptors have been determined, named M1-M5 (using an upper case M and subscript number). M1, M3, M5 receptors are coupled with Gq proteins, while M2 and M4 receptors are coupled with Gi/o proteins.

M4 muscarinic receptors are coupled to Gi/o heterotrimeric proteins. They function as inhibitory autoreceptors for acetylcholine. Activation of M4 receptors inhibits acetylcholine release in the striatum. The M2 subtype of acetylcholine receptor functions similarly as an inhibitory autoreceptor to acetylcholine release, albeit functioning actively primarily in the hippocampus and cerebral cortex. Muscarinic acetylcholine receptors possess a regulatory effect on dopaminergic neurotransmission. Activation of M4 receptors in the striatum inhibit D1-induced locomotor stimulation in mice. M4 receptor-deficient mice exhibit increased locomotor simulation in response to D1 agonists, amphetamine and cocaine. Neurotransmission in the striatum influences extrapyramidal motor control, thus alterations in M4 activity may contribute to conditions such as Parkinson’s Disease. [Muscarinic acetylcholine receptor M4, https://en.wikipedia.org/w/index.php?title=Muscarinic_acetylcholine_receptor_M4&oldid=914772257 (last visited Oct. 1, 2019).]

References:
1) K. Shiozaki, E. Iseki, H. Uchiyama, Y. Watanabe, T. Haga, K. Kameyama, T. Yamada, T. Yamamoto, K. Kosaka Alterations of muscarinic acetylcholine receptor subtypes in diffuse Lewy body disease: relation to Alzheimer’s’s disease J Neurol Neurosurg Psychiatry. 1999 Aug; 67 (2): 209-13.
2) Kazumasa Shiozaki, Eizo Iseki, Hiroaki Hino, Kenji Kosaka Distribution of m1 acetylcholine receptors in the hippocampus of patients with patients and patients with dementia with Lewy bodies-an immunohistochemistry study J Neurol Sci. 2001 Dec 15.

Application: IF, WB

Clonality: Monoclonal

Host: Mouse

Purification: Ammonium Sulfate

Reactivity: Mouse, Human

Nucleotide excision repair (NER) is a major repair system for removing a variety of DNA lesions including UV-induced cyclobutane pyrimidine dimers and (6-4) photoproducts as well as chemically-induced bulky base adducts. Defects in the NER system give rise to xeroderma pigmentosum (XP), an autosomal recessive disease characterized by a predisposition to skin cancer and in some cases neurological abnormalities. The early process of human NER, from damage recognition to dual incision (removal of damage-containing oligonucleotides), is accomplished by six core NER factors, XPC-RAD23B, TFIIH, XPA, RPA, XPF-ERCC1 and XPG.

XPF harbors a nuclease domain and forms a stable complex with ERCC1. The ERCC1-XPF complex has a unique ability to make a nick on the DNA strand which makes the transition from duplex to single-stranded DNA in the 5′ to 3′ direction. In the NER process, ERCC1-XPF is responsible for 5′-incision at a dual incision step.

Application: IHC(f), IF

Clonality: Polyclonal

Conjugation: Fluorescein

Host: Rabbit

Purification: Ig-PG

Reactivity: Streptococcus

Acute post-streptococcal glomerulonephritis (APSGN) is an infection- triggered glomerulonephritic disease (Reference 1). Nephritis-Associated Plasmin receptor (NAPlr) is an intracellular component of hemolytic streptococcus that induces nephritis. Glomerular NAPlr deposition is frequently found in infection-related glomerulonephritis (IRGN), especially in glomerulonephritis that is triggered by streptococcal infection (i.e. streptococcal-infection related nephritis [SIRN]). Glomerular NAPlr deposition is not found in non-infection-related nephritis.

Therefore, Immunostaining using anti-NAPlr antibody is ideal for identifying IRGN and SIRN (References 2-5). Although a distinct commercially available anti-NAPlr monoclonal antibody (1F10) has been in use, it is claimed to suffer from low sensitivity in Immunostaining. By contrast, staining sensitivity is better with polyclonal anti-NAPlr antibodies. However, stable generation and supply of this pAb is difficult because of the complicated step of NAPlr extraction from streptococcal particles. This new polyclonal antibody against an NAPlr peptide was established to balance both satisfactory sensitivity in Immunostaining with stable antibody production.

References:
1) Oda T, Up-to-date findings on infection-related glomerulonephritis. æ±åŒ»å¤§èªŒ73(4):355-363, 2015.
2) Yoshizawa N, Yamakami K, Fujino M, et al. (2004) Nephritis-associated plasmin receptor and acute poststreptococcal glomerulonephritis. J Am Soc Nephrol. 15:1785-93.
3) Oda T, Yamakami K, Yoshizawa N, et al. (2005) Glomerular plasmin-like activity in relation to nephritis-associated plasmin receptor in acute poststreptococcal glomerulonephritis. J Am Soc Nephrol. 16:247-54.
4) Oda T, Yoshizawa N, Yamakami K, et al. (2010) Localization of nephritis-associated plasmin receptor in acute poststreptococcal glomerulonephritis. Hum Pathol. 41(9):1276-85.
5) Oda T, Yoshizawa N, Yamakami K, et al. (2012) The role of nephritis-associated plasmin receptor (NAPlr) in glomerulonephritis associated with streptococcal infection. J Biomed Biotechnol. 2012:417675.

Application: ELISA, IHC(p), WB

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Bovine, Human

Versican (also known as PG-M), encoded by the VCAN/CSPG2 gene, is a large extracellular matrix chondroitin sulfate proteoglycan ubiquitously expressed in interstitial matrices of the human body, including brain ECM. It was first described in the bovine aorta by the research groups of Dick Heinegard and Anders Malmstrom’s groups (1982) and shortly after isolated from the chick embryo by Koji Kimata’s group. Cloning of the human VCAN/CSPG2 gene was accomplished in 1989 by Zimmermann and Ruoslahti, who also named the protein as versican in recognition of its versatile modular structure. Versican belongs to the lectican proteoglycan subgroup, to which aggrecan, brevican and neurocan also belong and share the N-terminal (G1) globular domain. This consists of Ig-like loops and two link modules and is responsible for the binding to hyaluronan, which may or may not be further stabilized by link proteins. At least 4 different alternatively spliced versican isoforms are known in higher vertebrates (denoted V0, V1, V2 and V3) while lower vertebrates may have additional ones in part by duplication of the gene. These isoforms are generated through differential utilization of the central core protein regions denoted GAG-α and GAG-β and encompass glycosaminoglycan (chondroitin sulfate) attachment sites. The V0 isoform is the parental one containing both the above “GAG-attachment” exons; the V1 isoform has only the GAG-β domain; the V2 isoform has only the GAG-α domain; and the V3 isoform is void of any GAG attachment domains, and is therefore a GAG-free proteoglycan. This implies that the versican isoform core proteins have a molecular mass range of 50-550 kDa and, when taking also into consideration the extensive glycosylation of the versican core protein, the molecular weights of the different isoforms vary from about 60 kDa to 1,500-2,000 kDa. The C-terminal (G3) globular domain consists of one or two EGF repeats, a C-type lectin module and complement regulatory protein (CRP)-like domain. The C-terminal domain binds a variety of ligands in the ECM and thereby contributes to the macromolecular organization of versican. The role of versican in ECM assembly of elastic matrices, cell adhesion, cell migration, and cell proliferation has been extensively described and its essential role during embryonic development is confirmed by early lethality of murine embryos homozygous for CSPG2 gene deletion. Like other large proteoglycans, versican is processed by multiple MMPs and ADAMTSs and its matrix deposition may be strongly down- or up-regulated in degenerative diseases and cancer. In some tumors its expression pattern has been proposed to have a prognostic value.

References:
1) Wight TN., Curr Opin Cell Biol.2002 Oct;14(5):617-23. PMID:12231358
2) Wu YJ, et all., Cell Res. 2005 Jul;15(7):483-94. PMID:16045811.
3) Cattaruzza S, et all., J Biol Chem. 2002 Dec 6;277(49):47626-35..PMID:12221092
4) Garusi E, et all., Cell Mol Life Sci. 2012 Feb;69(4):553-79. PMID:21964924
5) Heinegard D, et all., Biochem J. 1985 Aug 15;230(1):181-94. PMID:4052035
6) Kimata K, et all., J Biol Chem.1986 Oct 15;261(29):13517-25. PMID:3759975
7) Morgelin M., et all., J Biol Chem.1989 Jul 15;264(20):12080-90. PMID:2745430
8) Zimmermann DR, et all., EMBO J. 1989 Oct;8(10):2975-81. PMID:2583089

Application: IHC(p)

Clonality: Monoclonal

Host: Mouse

Purification: Ascities

Reactivity: Mouse, Rat, Human

Myelin is a lipid-rich (fatty) substance formed in the central nervous system (CNS) by glial cells called oligodendrocytes, and in the peripheral nervous system (PNS) by Schwann cells. Myelin insulates nerve cell axons to increase the speed at which information (encoded as an electrical signal) travels from one nerve cell body to another (as in the CNS) or, for example, from a nerve cell body to a muscle (as in the PNS). The myelinated axon can be likened to an electrical wire (the axon) with insulating material (myelin) around it. However, unlike the plastic covering on an electrical wire, myelin does not form a single long sheath over the entire length of the axon. Rather, each myelin sheath insulates the axon over a single section and, in general, each axon comprises multiple long myelinated sections separated from each other by short gaps called Nodes of Ranvier. Each myelin sheath is formed by the concentric wrapping of an oligodendrocyte or Schwann cell process around the axon. More precisely, myelin speeds the transmission of electrical impulses called action potentials along myelinated axons by insulating the axon and reducing axonal membrane capacitance. On a molecular level, it increases the distance between the cations on the outside of the axon and the Na⁺ ions that move through the axoplasm during an action potential, thereby greatly reducing the magnitude of the repulsive forces (which are inversely proportional to the square of the distance, as per Coulomb’s law) between them that would otherwise act to inhibit the movement of the Na⁺-ions. The discontinuous structure of the myelin sheath results in saltatory conduction[1][2] whereby the action potential “jumps” from one node of Ranvier, over a long myelinated stretch of the axon called the internode, before “recharging” at the next node of Ranvier, and so on, until it reaches the axon terminal. Nodes of Ranvier are the short (~1 micron) unmyelinated regions of the axon between adjacent long (~0.2 mm – >1 mm) myelinated internodes. Once it reaches the axon terminal, this electrical signal provokes the release of a chemical message or neurotransmitter that binds to receptors on the adjacent post-synaptic cell (e.g. nerve cell in the CNS or muscle cell in the PNS) at specialized regions called synapses. This “insulating” role for myelin is essential for normal motor function (i.e. movement such as walking), sensory function (e.g. hearing, seeing or feeling the sensation of pain) and cognition (e.g. acquiring and recalling knowledge), as demonstrated by the consequences of disorders that affect it, such as the genetically determined leukodystrophies;[3] the acquired inflammatory demyelinating disorder, multiple sclerosis;[4] and the inflammatory demyelinating peripheral neuropathies.[5] Due to its high prevalence, multiple sclerosis, which specifically affects the central nervous system (brain, spinal cord and optic nerve), is the best known disorder of myelin. [from: Wikipedia contributors. (2019, June 2). Myelin. In Wikipedia, The Free Encyclopedia. Retrieved 20:18, June 4, 2019, from https://en.wikipedia.org/w/index.php?title=Myelin&oldid=899981120]

References:
1) Nakazato Y, et al.: Monoclonal antibodies which recognize phosphorylated and nonphosphorylated epitopes of neurofilament protein. Biomed Res 1987, 8:369-376.
2) Arai H, et al. (1998) A novel marker of Schwann cells and myelin of the peripheral nervous system. Pathology Int. 48:206-214.
3) 新井華子, 他 (1998) シュワン細胞と末梢性髄鞘の新しいマーカー(Schwann/2E 抗体)によるシュワン細胞由来腫瘍の検索. Kitakanto Med. J. 48:1-8.
4) Jasmin L, et a. (2000) Schwann cells are removed from the spinal cord after effecting recovery from paraplegia. J Neurosci. 20:9215-9223.
5) Jasmin L, et al. (2002) Remyelination within the CNS: do schwann cells pave the way for oligodendrocytes? Neuroscientist

Application: ELISA, IP, WB

Clonality: Monoclonal

Conjugation: Biotin

Host: Mouse

Purification: Ig-PG

Reactivity: Human

CD63 (also known as LAMP-3, Melanoma-associated antigen ME491, TSPAN30, MLA1 and OMA81H) is a cell surface glycoprotein which belongs to the tetraspanin superfamily. CD63 is known to complex with integrins. CD63 is expressed on activated platelets, monocytes and macrophages, and is weakly expressed on granulocytes, T cells and B cells. Importantly, it is found on the surface of exosomes.

Exosomes are cell-derived vesicles bounded by a lipid bilayer membrane and exhibiting a diameter of 50 to 150 nm. They are secreted from cultured cells and are observed in body fluids such as saliva, blood, urine, amniotic fluid, malignant ascites. Recent studies indicate that exosomes contain various proteins and RNAs, suggesting a role in information transfer between cells.

This monoclonal antibody can be used to immunoprecipitate exosomes from serum and culture supernatants.

References:
1) Yoshioka Y et al., Nat Commun. 2014 Apr 7;5:3591. doi: 10.1038/ncomms4591.
2) N Nishida-Aoki et al., Mol Ther. 2017 Jan 4;25(1):181-191. doi: 10.1016/j.ymthe.2016.10.009.
3) Saito S et al., Sci Rep. 2018 Mar 5;8(1):3997. doi: 10.1038/s41598-018-22450-2.

Application: IHC(p), WB, IHC(f), IP

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Rat, Other Animals

Neurocan is a nervous tissue-unique, secretory proteoglycan that carries predominantly chondroitin sulfate side chains. Its expression gradually decreases with nervous tissue development. In the immature brain, neurocan exists in a full-length form with a 240 kDa-core glycoprotein, whereas in the mature brain it exists as proteolytic fragments of the NH2-terminal half (neurocan-N) with a 130 kDa-core glycopeptide and the COOH-terminal half (neurocan-C) with a 150 kDa-core glycopeptide. Neurocan is implicated in neural network formation and is a susceptibility factor for bipolar disorder. It is upregulated in central nervous system lesion sites and is a major component of glial scars. This antibody effectively recognizes the COOH-terminal half of rat neurocan core glycoprotein as well as the full length neurocan core glycoprotein.

References:
1) Oohira, A. et al. (1994) Neuroscience. 60:145-157. PMID: 8052408.
2) Matsui, F. et al. (1994) Neurochem. Int. 25:425-431.
3) Watanabe, E. et al. (1995) Eur. J. Neurosci. 7:547-554.
4) Fukuda, T. et al. (1997) J. Comp. Neurol. 382:141-152.
5) Inatani, M. et al. (1999) Invest. Ophthalmol. Vis. Sci. 40:2350-2359.

Application: IP, IF, WB, IHC(f)

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Porcine, Rabbit, Bovine, Human

This gene encodes the alpha chain of type VII collagen. The type VII collagen fibril, composed of three identical alpha collagen chains, is restricted to the basement zone beneath stratified squamous epithelia. It functions as an anchoring fibril between the external epithelia and the underlying stroma. Mutations in this gene are associated with all forms of dystrophic epidermolysis bullosa. The inherited disease, dystrophic epidermolysis bullosa, is caused by recessive or dominant mutations in COL7A1. In the absence of mutations, however, an autoimmune response against type VII collagen can result in an acquired form of this disease called epidermolysis bullosa acquisita. Type VII collagen is also found in the retina; its function in this organ is unknown. Collagen, type VII, alpha 1 has been shown to interact with Laminin 5 and Fibronectin.

Source: Nagoya University Graduate School of Science Department of Life Science Cell Biology Group Lecturer Mr. Yoshiko Hirako

References:
1) Uematsu J., et al. Eur J Cell Biol., 84: 407-415 (2005).
2) Hirako Y., et al. J. Biol. Chem., 273:9711-9717 (1998).

Application: ELISA, IHC, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Rat, Human

Application: IHC, Neutralization, RIA

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Chicken

Gonadotropin Releasing Hormone (GnRH), also know as Luteinizing-hormone-releasing-hormone (LHRH) and luliberin, is a tropic peptide hormone responsible for the release of follicle-stimulating hormone (FSH) and Luteinizing Hormone (LH) from the anterior pituitary. GnRH is synthesized and released from neurons within the hypothalamus. The peptide belongs to gonadotropin-releasing hormone family.

Application: IP, ELISA, IHC(p), WB

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Human

Aggrecan is the major proteoglycan in the articular cartilage (synthesized by mature chondrocytes) and in perineuronal nets of the CNS. While its precise function around CNS neurons remains obscure, in articular cartilage it contributes to creating the hydrated gel structure of the ECM via its interaction with hyaluronan, link protein, CMPs, COMP and collagen type IX. Deletion of the aggrecan gene causes early disturbances in chondrogenesis and brain defects. Aggrecan is a multimodular molecule whose core protein is composed of three globular domains denoted G1, G2, and G3, a large extended region spanning the portion of the molecule between the globular domains G1 and G2 and containing the majority of the GAG attachment sites and a second GAG-bearing inter-globular domain (IGD) occurs between G2 and G3. The GAG attachment domain between G1 and G2 contains mainly chondroitin sulphate chains (up to 40) and some keratan sulfate chains. The inter-globular G2-G3 domain exclusively bears keratan sulphate chains. The corresponding core protein region of sclera and brain aggrecans do not seem to contain keratan sulphates. The G1 amino-terminal domain of the aggrecan core protein has the same structural motif as link protein and is responsible for the binding of the proteoglycan to hyaluronan and link protein. The G2 globular domain is homologous to the tandem repeats of G1 and of link protein and is crucial for the synthesis and cellular secretion of aggrecan. The G3 globular domain makes up the carboxyl terminus of the core protein and is similarly responsible for post-translational processing of the proteoglycan and its secretion, as well as for its molecular interactions with other cartilage ECM components. Fully glycosylated/glycanated aggrecan of articular cartilage has an average size of 2,400-2,500 kDa, but its Mr may vary with age and the conditions of the cartilage tissue. The non-glycosylated/non-glycanated core protein has an approximate Mr of 240 kDa.

References:
Virgintino D, et all., (2009) Aggrecan isoforms of perineuronal nets identify subsets of parvalbumin and calbindin neurons differentially distributed in cortical layers II-VI of human adult cortex. J. Cell. Mol. Medicine 13, 3151-3173.I161:I164.

Application: IP

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Rat, Human

Muscarinic acetylcholine receptors, or mAChRs, are acetylcholine receptors that form G protein-coupled receptor complexes in the cell membranes of certain neurons and other cells. They play several roles, including acting as the main end-receptor stimulated by acetylcholine released from postganglionic fibers in the parasympathetic nervous system. Muscarinic receptors are so named because they are more sensitive to muscarine than to nicotine. By the use of selective radioactively labeled agonist and antagonist substances, five subtypes of muscarinic receptors have been determined, named M1-M5 (using an upper case M and subscript number). M1, M3, M5 receptors are coupled with Gq proteins, while M2 and M4 receptors are coupled with Gi/o proteins.

M3 receptor: The M3 muscarinic receptors are located at many places in the body. They are located in the smooth muscles of the blood vessels, as well as in the lungs. Because the M3 receptor is Gq-coupled and mediates an increase in intracellular calcium, it typically causes contraction of smooth muscle, such as that observed during bronchoconstriction and bladder voiding. However, with respect to vasculature, activation of M3 on vascular endothelial cells causes increased synthesis of nitric oxide, which diffuses to adjacent vascular smooth muscle cells and causes their relaxation, thereby explaining the paradoxical effect of parasympathomimetics on vascular tone and bronchiolar tone. Indeed, direct stimulation of vascular smooth muscle, M3 mediates vasconstriction in pathologies wherein the vascular endothelium is disrupted. The M3 receptors are also located in many glands, which help to stimulate secretion in, for example, the salivary glands, as well as other glands of the body.

References:
1) K. Shiozaki, E. Iseki, H. Uchiyama, Y. Watanabe, T. Haga, K. Kameyama, T. Yamada, T. Yamamoto, K. Kosaka Alterations of muscarinic acetylcholine receptor subtypes in diffuse Lewy body disease: relation to Alzheimer’s’s disease J Neurol Neurosurg Psychiatry. 1999 Aug; 67 (2): 209-13.
2) Kazumasa Shiozaki, Eizo Iseki, Hiroaki Hino, Kenji Kosaka Distribution of m1 acetylcholine receptors in the hippocampus of patients with patients and patients with dementia with Lewy bodies-an immunohistochemistry study J Neurol Sci. 2001 Dec 15

Application: IP, ELISA, IHC(p), WB

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Human, Bovine

Aggrecan is the major proteoglycan in the articular cartilage (synthesized by mature chondrocytes) and in perineuronal nets of the CNS. While its precise function around CNS neurons remains obscure, in articular cartilage it contributes to creating the hydrated gel structure of the ECM via its interaction with hyaluronan, link protein, CMPs, COMP and collagen type IX. Deletion of the aggrecan gene causes early disturbances in chondrogenesis and brain defects. Aggrecan is a multimodular molecule whose core protein is composed of three globular domains denoted G1, G2, and G3, a large extended region spanning the portion of the molecule between the globular domains G1 and G2 and containing the majority of the GAG attachment sites and a second GAG-bearing inter-globular domain (IGD) occurs between G2 and G3. The GAG attachment domain between G1 and G2 contains mainly chondroitin sulphate chains (up to 40) and some keratan sulfate chains. The inter-globular G2-G3 domain exclusively bears keratan sulphate chains. The corresponding core protein region of sclera and brain aggrecans do not seem to contain keratan sulphates. The G1 amino-terminal domain of the aggrecan core protein has the same structural motif as link protein and is responsible for the binding of the proteoglycan to hyaluronan and link protein. The G2 globular domain is homologous to the tandem repeats of G1 and of link protein and is crucial for the synthesis and cellular secretion of aggrecan. The G3 globular domain makes up the carboxyl terminus of the core protein and is similarly responsible for post-translational processing of the proteoglycan and its secretion, as well as for its molecular interactions with other cartilage ECM components. Fully glycosylated/glycanated aggrecan of articular cartilage has an average size of 2,400-2,500 kDa, but its Mr may vary with age and the conditions of the cartilage tissue. The non-glycosylated/non-glycanated core protein has an approximate Mr of 240 kDa.

References:
Virgintino D, et all., (2009) Aggrecan isoforms of perineuronal nets identify subsets of parvalbumin and calbindin neurons differentially distributed in cortical layers II-VI of human adult cortex. J. Cell. Mol. Medicine 13, 3151-3173.I161:I164

Application: IP

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Porcine, Human

Muscarinic acetylcholine receptors, or mAChRs, are acetylcholine receptors that form G protein-coupled receptor complexes in the cell membranes of certain neurons and other cells. They play several roles, including acting as the main end-receptor stimulated by acetylcholine released from postganglionic fibers in the parasympathetic nervous system. Muscarinic receptors are so named because they are more sensitive to muscarine than to nicotine. By the use of selective radioactively labeled agonist and antagonist substances, five subtypes of muscarinic receptors have been determined, named M1-M5 (using an upper case M and subscript number). M1, M3, M5 receptors are coupled with Gq proteins, while M2 and M4 receptors are coupled with Gi/o proteins.

M2 receptor: The M2 muscarinic receptors are located in the heart, where they act to slow the heart rate down to normal sinus rhythm, by slowing the speed of depolarization. In humans under resting conditions vagal activity dominates over sympathetic activity. Hence inhibition of m2 receptors (e.g. by atropine) will cause a raise in heart rate. They also moderately reduce contractile forces of the atrial cardiac muscle, and reduce conduction velocity of the atrioventricular node (AV node). It also serves to slightly decrease the contractile forces of the ventricular muscle.

References:
1) K. Shiozaki, E. Iseki, H. Uchiyama, Y. Watanabe, T. Haga, K. Kameyama, T. Yamada, T. Yamamoto, K. Kosaka Alterations of muscarinic acetylcholine receptor subtypes in diffuse Lewy body disease: relation to Alzheimer’s’s disease J Neurol Neurosurg Psychiatry. 1999 Aug; 67 (2): 209-13. ​​​​
​​2) Kazumasa Shiozaki, Eizo Iseki, Hiroaki Hino, Kenji Kosaka Distribution of m1 acetylcholine receptors in the hippocampus of patients with patients and patients with dementia with Lewy bodies-an immunohistochemistry study J Neurol Sci. 2001 Dec 15.

Application: IP, IF, WB, IHC(f)

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Rabbit, Bovine, Human

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituents of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are heterotrimers composed of 3 non-identical chains that adopt a cruciform structure with 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene and in some cases undergoes alternative splicing to give rise to separate chain variants.

References:
1) Hirako Y., Yoshino K., Zillikens D., Owaribe K. Extracellular cleavage of bullous pemphigoid antigen 180/type XVII collagen and its involvement in hemidesmosomal disassembly. J Biochem. 2003 Feb;133(2):197-206. PMID: 12761182
2) Uematsu J., Nishizawa Y., Hirako Y., Kitamura K., Usukura J., Miyata T., Owaribe K. Both type-I hemidesmosomes and adherens-type junctions contribute to the cell-substratum adhesion system in myoepithelial cells. Eur J Cell Biol. 2005 Mar;84(2-3):407-15. PMID: 15819417
3) Owaribe K, Nishizawa Y, Franke WW. Isolation and characterization of hemidesmosomes from bovine corneal epithelial cells. Exp Cell Res. 1991 Feb;192(2):622-30. PMID:1988297

Application: ELISA, IHC

Clonality: Polyclonal

Host: Rabbit

Reactivity: All

8-Nitroguanosine is a nitrated nucleic acid which is formed by peroxynitrite, myeloperoxidase, nitrite, and peroxide. It is known that nitration of guanine is enhanced in virus infection (1, 2), bacterial infection (3, 4), inflammatory disease (5), cancer (5), and diseases associated with smoking (6). 8-nitroguanosine is thought to be a DNA damage marker created by oxidative stress. Cyclic GMP (cGMP) is an important signaling molecule. Interestingly, 8-Nitro-cGMP (nitrated cGMP) has been identified in vivo (3). Therefore, 8-Nitro-cGMP could potentially act as a mediator for reactive oxygen signaling (3, 7-9).

Anti-Nitroguanosine polyclonal antibody does not cross-react with normal nucleobases but selectively reacts with nitrated nucleic acids such as nitroguanosine, nitroguanine, and nitroxanthine. Therefore, Anti-Nitroguanosine polyclonal antibody is a universal antibody against guanine modified 8th position with a nitro group. Anti-Nitroguanosine polyclonal antibody has very high affinity for 8-nitroguanine and 8-nitroguanosine, but it does not cross-react with normal guanosine, guanine, 8-hydroxyguanine or 3-nitrotyrosine. Since this antibody was prepared using rabbits, it can be used for immuno-histostaining of rodent tissues.

References:
1) T. Akaike, S. Okamoto, T. Sawa, J. Yoshitake, F. Tamura, K. Ichimori, K. Miyazaki, K. Sasamoto and H. Maeda, 8-nitroguanosine formation in viral pneumonia and its implication for pathogenesis, Proc. Natl. Acad. Sci. USA, 100, 685-690 (2003).
2) J. Yoshitake, T. Akaike, T. Akuta, F. Tamura, T. Ogura, H. Esumi, and H. Maeda, Nitric oxide as an endogenous mutagen for Sendai virus without antiviral activity, J. Virol., 78, 8709-8719 (2004).
3) T. Sawa, M. H. Zaki, T. Okamoto, T. Akuta, Y. Tokutomi, S. Kim-Mitsuyama, H. Ihara, A. Kobayashi, M. Yamamoto, S. Fujii, H. Arimoto, and T. Akaike, Protein S-guanylation by the biological signal 8-nitroguanosine 3′,5′-cyclic monophosphate, Nat. Chem. Biol., 3, 727-735 (2007).
4) M. H.Zaki, S. Fujii, T. Okamoto, S. Islam, S. Khan, K. A. Ahmed, T. Sawa, and T. Akaike, Cytoprotective function of heme oxygenase 1 induced by a nitrated cyclic nucleotide formed during murine salmonellosis, J. Immunol., 182, 3746-3756 (2009).
5) Y. Terasaki, T. Akuta, M. Terasaki, T. Sawa, T. Mori, T. Okamoto, M. Ozaki, M. Takeya and T. Akaike, Guanine nitration in idiopathic pulmonary fibrosis and its implication for carcinogenesis, Am. J. Respir. Crit. Care. Med., 174, 665-673 (2006).
6) T. Sawa, M. Tatemichi, T. Akaike, A. Barbin and H. Ohshima, Analysis of urinary 8-nitroguanine, a marker of nitrative nucleic acid damage, by high-performance liquid chromatography-electrochemical detection coupled with immunoaffinity purification: association with cigarette smoking, Free Radic. Biol. Med., 40, 711-720 (2006).
7) M. Feelisch, Nitrated cyclic GMP as a new cellular signal, Nat. Chem. Biol., 3, 687-688 (2007).
8) K. A. Ahmed, T. Sawa, T. Akaike, Protein cysteine S-guanylation and electrophilic signal transduction by endogeneous nitro-nucleotides, Amino Acids (2010).
9) T. Sawa, H. Arimoto and T. Akaike, Regulation of redox signaling involving chemical conjugation of protein thiols by nitric oxide and electrophiles, Bioconjugate Chem (2010).

Application: FC, IHC, IF

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Mouse

Translocator protein (TSPO) is an 18 kDa protein mainly found on the outer mitochondrial membrane. It was first described as peripheral benzodiazepine receptor (PBR), a secondary binding site for diazepam, but subsequent research has found the receptor to be expressed throughout the body and brain.[5] In humans, the translocator protein is encoded by the TSPO gene.[6][7] It belongs to family of tryptophan-rich sensory proteins. Regarding intramitochondrial cholesterol transport, TSPO has been proposed to interact with StAR (steroidogenic acute regulatory protein) to transport cholesterol into mitochondria, though evidence is mixed.[8] In animals, TSPO (PBR) is a mitochondrial protein usually located in the outer mitochondrial membrane and characterized by its ability to bind a variety of benzodiazepine-like drugs, as well as to dicarboxylic tetrapyrrole intermediates of the haem biosynthetic pathway. TSPO has many proposed functions depending on the tissue.[9] The most studied of these include roles in the immune response, steroid synthesis and apoptosis. [from: Wikipedia contributors. (2019, April 29). Translocator protein. In Wikipedia, The Free Encyclopedia. Retrieved 18:37, June 4, 2019, from https://en.wikipedia.org/w/index.php?title=Translocator_protein&oldid=894679824]

Application: IHC, WB, ICC, IF

Clonality: Monoclonal

Host: Rat

Purification: IgG

Reactivity: Monkey, Mouse, Rat, Human

Prohibitin, also known as PHB, is a protein that in humans is encoded by the PHB gene.[5] The Phb gene has also been described in animals, fungi, plants, and unicellular eukaryotes. Prohibitins are divided in two classes, termed Type-I and Type-II prohibitins, based on their similarity to yeast PHB1 and PHB2, respectively. Each organism has at least one copy of each type of prohibitin gene.[6][7] Prohibitins are evolutionarily conserved genes that are ubiquitously expressed. The human prohibitin gene, located on the BRCA1 chromosome region 17q21, was originally thought to be a negative regulator of cell proliferation and a tumor suppressor. This anti-proliferative activity was later attributed to the 3′ UTR of the PHB gene, and not to the actual protein. Mutations in human PHB have been linked to sporadic breast cancer. However, over-expression of PHB has been associated with a reduction in the androgen receptor activity and a reduction in PSA gene expression resulting in a decrease of androgen-dependent growth of cancerous prostate cells.[8] Prohibitin is expressed as two transcripts with varying lengths of 3′ untranslated region. The longer transcript is present at higher levels in proliferating tissues and cells, suggesting that this longer 3′ untranslated region may function as a trans-acting regulatory RNA.[5] Prohibitins are assembled into a ring-like structure with 16–20 alternating Phb1 and Phb2 subunits in the inner mitochondrial membrane.[9] The precise molecular function of the PHB complex is not clear, but a role as chaperone for respiration chain proteins or as a general structuring scaffold required for optimal mitochondrial morphology and function are suspected. Recently, prohibitins have been demonstrated to be positive, rather than negative, regulators of cell proliferation in both plants and mice. Both human prohibitins have also been suggested to be localized in the nucleus and modulate transcriptional activity by interacting with various transcription factors, including nuclear receptors, either directly or indirectly. However, little evidence for nuclear targeting and transcription factor-binding of prohibitins has been found in other organisms (yeast, plants, C. elegans, etc.), indicating that this may be a specific function in mammalian cells.[10][11][12][13] [from: Wikipedia contributors. (2019, February 20). Prohibitin. In Wikipedia, The Free Encyclopedia. Retrieved 18:24, June 4, 2019, from https://en.wikipedia.org/w/index.php?title=Prohibitin&oldid=884240489]

References:
1) Sun et al. (2011) CaMK IV phosphorylates prohibitin 2 and regulates prohibitin 2-mediated repression of MEF2 transcription. Cell Signal. 23:1686-1690.

Application: IP, ELISA, IHC(p)

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Human, Bovine

Biglycan is a small secreted ECM proteoglycan belonging to the small leucine-rich repeat (SLRP) subfamily. It contains a central 12 LRR domain flanked by small cysteine clusters at either side. The structure of biglycan core protein is highly conserved across species; over 90% has been reported for rat, mouse, bovine and human biglycan core proteins. Two glycosaminoglycan chains of the chondroitin or dermatan sulfate type are attached near the amino terminus of the core protein, generating a molecule that in its fully glycanated form reaches 250 kDa. Deposition of non-glycanated forms of biglycan have been shown to increase in cartilage and bone ECMs with age. Like decorin and fibromodulin, biglycan controls collagen fibrillogenesis and, partly through this action, it is believed to play a key role in bone mineralization and the assembly of cartilage and corneal ECM. In fact, deletion of the biglycan gene leads to an osteoporosis-like phenotype and double knockout of biglycan and fibromodulin cause severe cartilage and macular degeneration. The biglycan core protein binds BMP4 and may influence its bioactivity, especially in the context of osteoblast differentiation/maturation. This is believed to depend upon the ability of biglycan to regulate the interaction of the growth factor with its extracellular antagonist chordin. There is also evidence that biglycan may bind TGFb1 and affect homeostasis and new formation of blood vessels. Furthermore, BGN may affect signal transduction during cell growth and differentiation via induction of the cyclin-dependent kinase inhibitor p27KIP1. Biglycan-induced activation of RhoA and Rac1 signaling increases migration of lung fibroblasts. Moreover, adenovirus-mediated gene transfer of BGN induced a fibroblastic response in the lung, indicating a role of BGN in fibrogenesis. Finally, biglycan is up-regulated during inflammation and augments this condition by contributing to Toll-like receptors 2 and 4 signaling in macrophages.

Application: ELISA, IHC

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: All

Monoclonal antibody 3B3 recognizes 6-sulfated unsaturated disaccharide neoepitopes (i.e. C-6-S “stubs”) generated at the non-reducing terminal of Chondroitin Sulfate glycosaminoglycan chains that have been pre-digested with either Chondroitinase ABC or Chondroitinase ACII. Monoclonal antibody 3B3 also recognizes a non-reducing end saturated disaccharide epitope in ‘native’ Chondroitin Sulfate glycosaminoglycan chains consisting of a terminal glucuronic acid adjacent to 6-sulfated N-acetyl-galactosamine. The chondroitinase-generated neoepitope is often denoted as 3B3(+) and the ‘native’ terminal epitope as 3B3(-) in publications [see Figure 2; Caterson B (2012) Int. J. Exp. Pathol. 93: 1 – 10].

References:
1) Schwend T, Deaton RJ, Zhang Y, Caterson B & Conrad CW (2012). Corneal sulphated glycosaminoglycans and their effects on trigeminal nerve growth cone behaviour in vitro – roles for ECM in corneal innervation. Invest Opthamol Vis Sci. 53:
2) Caterson B. (2012). Chondroitin sulphate glycosaminoglycans: fun for some and confusion for others. Int. J. of Exp. Path. 93: 1 – 10 PubMed: 22264297
3) Liles M, Palka BP, Harris A,Kerr BC, Hughes CE, Young RD, Meek KM, Caterson B, Quantok AJ (2010). Differential relative sulphation of keratan sulphate glycosaminoglycan in the chick cornea during embryonic development. Invest. Opthalmol. Vis. Sci. 51: 1365-1372 PubMed: 19815728
4) Davies L, Blain E, Caterson B and Duance VC (2008). Chondroitin sulphate impedes the migration of a sub-population of articular cartilage chondrocytes. Osteoarthritis & Cartilage 16: 855 – 864 PubMed: 18222711
5) Hayes AJ, Hughes CE & Caterson B (2008). Antibodies and immunohistochemistry in extracellular matrix research. Methods 45: 10 – 21 PubMed: 18442701
6) Hayes AJ, Hall A, Brown L, Tubo R & Caterson B (2007). Macromolecular organization and in vitro growth characteristics of scaffold-free neocartilage grafts. J. Histochem. Cytochem. 55: 853 – 866. PubMed: 17478447
7) Caterson B, Mahmoodian F, Sorrell JM, Hardingham TE, Bayliss MT, Carney SL, Ratcliffe A & Muir H (1990). Modulation of native chondroitin sulfate structure in tissue development and in disease. J. Cell Sci. 97: 411 – 417. PubMed: 1705939
8) Mehmet H, Scudder P, Tang, PW, Hounsell, EF, Caterson, B & Feizi T (1986). Antigenic determinants recognized by three monoclonal antibodies to keratan sulfate involve sulfated hepta- or larger oligosaccharides of the poly-N-acetyllactosamine series. Eur. J. Biochem. 157: 385 – 391. PubMed: 2423332
9) Funderburgh JL, Caterson B & Conrad GW (1986). Keratan sulfate proteoglycan during embryonic development of the chicken cornea. Developmental Biology 116: 267 – 277 PubMed: 2942429
10) Katz H, Austen KF, Caterson B, & Stevens RL (1986). Secretory granules of Heparin-containing Rat serosal mast cells also possess highly sulfated chondroitin sulfate proteoglycans. J. Biol. Chem. 261: 13393 – 13396 PubMed: 3531203
11) Caterson B, Christner JE, Baker JR & Couchman JR (1985). The production and characterization of monoclonal antibodies directed against connective tissue proteoglycans. Federation Proceedings 44: 386 – 393. PubMed: 257841
12) Couchman JR, Caterson B, Christner JE & Baker JR (1984). Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues. Nature 307: 650 – 652. PubMed: 6420711
13) Caterson B, Christner JE & Baker JR (1983). Identification of a monoclonal antibody that specifically recognizes corneal and skeletal keratan sulfate. Monoclonal antibodies to cartilage proteoglycan. J. Biol. Chem. 258: 8848 – 8854 PubMed: 6223038

Cosmo Bio抗体,Cosmo Bio,Anti Amyloid-Beta Precursor Protein (APP) mAb (Clone 278),CAC-YCU-MK-AP01

Application: ELISA, WB

Clonality: Monoclonal

Host: Mouse

Purification: Purified – Affinity

Reactivity: Human

Cosmo Bio抗体,Cosmo Bio

Application: ELISA, IF, IEM, FC, ICC

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

In neurons, the plasma membrane is functionally separated into several distinct segments. Neurons form these domains by delivering selected components to and by confining them within each segment of the membrane. Although some mechanisms of the delivery are elucidated, that of the confinement is unclear.We show here that 1-oleoyl-2-palmitoyl-phosphatidylcholine (OPPC),a unique molecular species of phospholipids, is concentrated at the protrusion tips of several neuronal culture cells and the presynaptic area of neuronal synapses of the mouse brain. InPC12 cells, NGF-stimulated neuronal differentiation induces a phospholipase A1 activity at the protrusion tips, which co-localizes with the OPPC domain. Inhibition of the phospholipase A1activity leads to suppression of phospholipid remodeling in the tip membrane and results in disappearance of the OPPC at the tips. In these cells, confinement of dopamine transporter and G0 proteins to the tip was also disrupted. These findings link the lateral distribution of the molecular species of phospholipids to the formation of functional segments in the plasma membrane of neurons and to the mechanism of protein confinement at the synapse.

The Cosmobio Antibody Collection (CAC) has registered a monoclonal antibody (clone 15-3C1) that specifically recognizes the phospholipid 1-Oleoyl-Palmitoyl-Phosphatidylcholine (OPPC) localized at neurite tips. Recently, Kuge et al found that OPPC controls protein localization (dopamine transport protein and G protein). This suggests that phospholipid remodeling is performed in the cell membrane, and that OPPC may play an important role in neurotransmission and be related to pathologies such as Parkinson’s disease and dementia.

Antibody Source: Professor Koichi Honke of Kochi University School of Medicine.
[from: Kuge, H., Akahori, K., Yagyu K., Honke K. Functional Compartmentalization of the Plasma Membrane of Neurons by a Unique Acyl Chain Composition of Phospholipids The Journal Of Biological Chemistry (2014) 289(39): 26783–26793.

Application: IHC, Neutralization, RIA

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human, Mouse, Rat, Bovine, Sheep

Application: IHC(p), WB, IF

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Mouse, Rat

Neurocan is a nervous tissue-unique, secretory proteoglycan that carries predominantly chondroitin sulfate side chains. Its expression gradually decreases with the nervous tissue development. In the immature brain, neurocan exists inafull-length form with a 240 kDa-core glycoprotein, whereas it exists totally in proteolytic fragments of the NH2-terminal half (neurocan-N) with a 130 kDa-core glycopeptide and the COOH-terminal half (neurocan-C) with a 150 kDa-core glycopeptide. Neurocan is implicated in the neural network formation, and is a susceptibility factor for bipolar disorder. This proteoglycan is upregulated in the lesion site of the central nervous system, and is a major component of the glial scar. In addition, neurocan-N, not neurocan-C, is detectable in the perineuronal nets of some neurons. This antibody recognizes effectively neurocan-N as well as the full-length neurocan.

References:
1) Oohira, A., Matsui, F., Tokita, Y., Yamauchi, S., & Aono, S., Molecular interactions of neural chondroitin sulfate proteoglycans in the brain development, (2000) Arch.Biochem.Biophys., 374, 24-34.
2) Fumiko Matsui, Masako Nishizuka, Yoko Yasuda, Sachiko Aono, Eiji Watanabe, Atsuhiko Oohira. Occurrence of a N-terminal proteolytic fragment of neurocan, not a C-terminal half, in a perineuronal net in the adult rat cerebrum, (1998) Brain Res., 790, 45-51
3) Matsui, F., Watanabe, E., & Oohira, A., Immunological identification of two proteglycan fragments derived from neurocan, a brain-specific chondroitin sulfate proteoglycan, (1994) Neurochem. Int., 25, 425-431.

Application: WB, IP, IHC

Clonality: Monoclonal

Host: Mouse

Purification: Purified – Affinity

Reactivity: Human

Lect1 encodes a glycosylated transmembrane protein that is cleaved to form a mature, secreted protein. The N-terminus of the precursor protein shares characteristics with other surfactant proteins and is sometimes called chondrosurfactant protein, although no biological activity has yet been defined for it. The C-terminus of the precursor protein contains a 25 kDa mature protein called leukocyte cell-derived chemotaxin-1 or chondromodulin-1. The mature protein promotes chondrocyte growth and inhibits angiogenesis. This gene is expressed in the avascular zone of prehypertrophic cartilage, and its expression decreases during chondrocyte hypertrophy and vascular invasion. The mature protein likely plays a role in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. It may also be involved in the broad control of tissue vascularization during development. Alternative splicing results in multiple transcript variants encoding different isoforms.[7] [from: Wikipedia contributors. (2017, October 27). LECT1. In Wikipedia, The Free Encyclopedia. Retrieved 17:42, June 3, 2019, from https://en.wikipedia.org/w/index.php?title=LECT1&oldid=807301938]

Application: IHC, WB, ELISA

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human, Mouse

Neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.

Alpha-Synuclein, a 140-amino acid protein abundantly expressed in presynaptic terminals, is a component of intraneuronal or glial inclusions observed in cases of Parkinson’s disease (PD), Dementia with Lewy bodies (DLB) and Multiple system atrophy (MSA). Although alpha-synuclein is a natively unfolded protein, fibrillization or conformational change(s) of alpha-synuclein is central to the pathogenesis of alpha-synucleinopathies. The amino-terminal region of alpha-synuclein consists of seven imperfect repeats, each 11 amino acids in length, with the consensus sequence KTKEGV. The repeats partially overlap with a hydrophobic region (amino acids 61-95). The carboxy-terminal region (amino acids 96-140) is negatively charged. These antibodies are powerful tools for biochemical and IHC analyses of neurodegenerative diseases and for evaluation of conformational changes of alpha-synuclein.

References:
1) Masami Masuda et al., Inhibition of a-synuclein fibril assembly by small molecules: Analysis using epitope-specific antibodies. FEBS Letters (2009) 583, 787-791. PMID 19183551
2) Motokuni Yonetani et al., Conversion of wild-type alpha-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. Journal of Biological Chemistry (2009) 284, 7940-7950. PMID 19164293

Application: ELISA, IHC(f), WB, IHC(p)

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Human, Bovine

Versican (also known as PG-M), encoded by the VCAN/CSPG2 gene, is a large extracellular matrix chondroitin sulfate proteoglycan ubiquitously expressed in interstitial matrices of the human body, including brain ECM. It was first described in the bovine aorta by the research groups of Dick Heinegard and Anders Malmstrom’s groups (1982) and shortly after isolated from the chick embryo by Koji Kimata’s group. Cloning of the human VCAN/CSPG2 gene was accomplished in 1989 by Zimmermann and Ruoslahti, who also named the protein as versican in recognition of its versatile modular structure. Versican belongs to the lectican proteoglycan subgroup, to which aggrecan, brevican and neurocan also belong and share the N-terminal (G1) globular domain. This consists of Ig-like loops and two link modules and is responsible for the binding to hyaluronan, which may or may not be further stabilized by link proteins. At least 4 different alternatively spliced versican isoforms are known in higher vertebrates (denoted V0, V1, V2 and V3) while lower vertebrates may have additional ones in part by duplication of the gene. These isoforms are generated through differential utilization of the central core protein regions denoted GAG-α and GAG-β and encompass glycosaminoglycan (chondroitin sulfate) attachment sites. The V0 isoform is the parental one containing both the above “GAG-attachment” exons; the V1 isoform has only the GAG-β domain; the V2 isoform has only the GAG-α domain; and the V3 isoform is void of any GAG attachment domains, and is therefore a GAG-free proteoglycan. This implies that the versican isoform core proteins have a molecular mass range of 50-550 kDa and, when taking also into consideration the extensive glycosylation of the versican core protein, the molecular weights of the different isoforms vary from about 60 kDa to 1,500-2,000 kDa. The C-terminal (G3) globular domain consists of one or two EGF repeats, a C-type lectin module and complement regulatory protein (CRP)-like domain. The C-terminal domain binds a variety of ligands in the ECM and thereby contributes to the macromolecular organization of versican. The role of versican in ECM assembly of elastic matrices, cell adhesion, cell migration, and cell proliferation has been extensively described and its essential role during embryonic development is confirmed by early lethality of murine embryos homozygous for CSPG2 gene deletion. Like other large proteoglycans, versican is processed by multiple MMPs and ADAMTSs and its matrix deposition may be strongly down- or up-regulated in degenerative diseases and cancer. In some tumors its expression pattern has been proposed to have a prognostic value.

References:
1) Mazzucato, M., et al., 2002. Vascular PG-M/versican variants promote platelet adhesion at low shear rates and cooperate with collagens to induce aggregation. FASEB J. 16, 1903-1916.
2) Cattaruzza S, et al., 2002. Distribution of PG-M/versican variants in human tissues and de novo expression of isoform V3 upon endothelial cell activation and neoangiogenesis. J.Biol.Chem.277, 47626-47635.
3) Cattaruzza S, Perris R. 2005. Proteoglycan control of cell movement during wound healing and cancer. Matrix Biol. 24, 400-417.

Application: ELISA, IF, WB

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Puromycin is an aminonucleoside antibiotic derived from the bacterial strain Streptomyces alboniger. Structurally resembling the 3′ end of aminoacyl-tRNAs, it can bind to translating ribosomes and cause premature chain termination. Classically, protein biosynthesis has been monitored using pulse-chase and flooding dose methods which both employ radioactive amino acid labels. Analysis using puromycin immunodetection is an advantageous alternative to radioactive amino acid labeling and allows for the direct evaluation/quantification of translation using standard immunochemical methods.

Features:
1) Easy to evaluate and quantify protein biosynthesis
2) An alternative to the traditional pulse-chase method that relies on radioactive amino acids
3) Applicable to Western blot and ELISA analyses

References:
1) Kelleher AR, Gordon BS, Kimball SR, Jefferson LS. Changes in REDD1, REDD2, and atrogene mRNA expression are prevented in skeletal muscle fixed in a stretched position during hindlimb immobilization. Physiol Rep. 2014 Feb 25;2(2):e00246. doi: 10.1002/phy2.246. eCollection 2014 Feb 1. PubMed PMID: 24744910; PubMed Central PMCID: PMC3966240.
2) Kelleher AR, Kimball SR, Dennis MD, Schilder RJ, Jefferson LS. The mTORC1 signaling repressors REDD1/2 are rapidly induced and activation of p70S6K1 by leucine is defective in skeletal muscle of an immobilized rat hindlimb. Am J Physiol Endocrinol Metab. 2013 Jan 15;304(2):E229-36. doi: 10.1152/ajpendo.00409.2012. PubMed PMID: 23193052; PubMed Central PMCID: PMC3543567.

Application: ELISA, IHC(p), WB

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Bovine, Human

Versican (also known as PG-M), encoded by the VCAN/CSPG2 gene, is a large extracellular matrix chondroitin sulfate proteoglycan ubiquitously expressed in interstitial matrices of the human body, including brain ECM. It was first described in the bovine aorta by the research groups of Dick Heinegard and Anders Malmstrom’s groups (1982) and shortly after isolated from the chick embryo by Koji Kimata’s group. Cloning of the human VCAN/CSPG2 gene was accomplished in 1989 by Zimmermann and Ruoslahti, who also named the protein as versican in recognition of its versatile modular structure. Versican belongs to the lectican proteoglycan subgroup, to which aggrecan, brevican and neurocan also belong and share the N-terminal (G1) globular domain. This consists of Ig-like loops and two link modules and is responsible for the binding to hyaluronan, which may or may not be further stabilized by link proteins. At least 4 different alternatively spliced versican isoforms are known in higher vertebrates (denoted V0, V1, V2 and V3) while lower vertebrates may have additional ones in part by duplication of the gene. These isoforms are generated through differential utilization of the central core protein regions denoted GAG-α and GAG-β and encompass glycosaminoglycan (chondroitin sulfate) attachment sites. The V0 isoform is the parental one containing both the above “GAG-attachment” exons; the V1 isoform has only the GAG-β domain; the V2 isoform has only the GAG-α domain; and the V3 isoform is void of any GAG attachment domains, and is therefore a GAG-free proteoglycan. This implies that the versican isoform core proteins have a molecular mass range of 50-550 kDa and, when taking also into consideration the extensive glycosylation of the versican core protein, the molecular weights of the different isoforms vary from about 60 kDa to 1,500-2,000 kDa. The C-terminal (G3) globular domain consists of one or two EGF repeats, a C-type lectin module and complement regulatory protein (CRP)-like domain. The C-terminal domain binds a variety of ligands in the ECM and thereby contributes to the macromolecular organization of versican. The role of versican in ECM assembly of elastic matrices, cell adhesion, cell migration, and cell proliferation has been extensively described and its essential role during embryonic development is confirmed by early lethality of murine embryos homozygous for CSPG2 gene deletion. Like other large proteoglycans, versican is processed by multiple MMPs and ADAMTSs and its matrix deposition may be strongly down- or up-regulated in degenerative diseases and cancer. In some tumors its expression pattern has been proposed to have a prognostic value.

References:

1) Wight TN., Curr Opin Cell Biol.2002 Oct;14(5):617-23. PMID:12231358

2) Wu YJ, et all., Cell Res. 2005 Jul;15(7):483-94. PMID:16045811.

3) Cattaruzza S, et all., J Biol Chem. 2002 Dec 6;277(49):47626-35..PMID:12221092

4) Garusi E, et all., Cell Mol Life Sci. 2012 Feb;69(4):553-79. PMID:21964924

5) Heinegard D, et all., Biochem J. 1985 Aug 15;230(1):181-94. PMID:4052035

6) Kimata K, et all., J Biol Chem.1986 Oct 15;261(29):13517-25. PMID:3759975

7) Morgelin M., et all., J Biol Chem.1989 Jul 15;264(20):12080-90. PMID:2745430

8) Zimmermann DR, et all., EMBO J. 1989 Oct;8(10):2975-81. PMID:2583089

Application: ELISA, IHC(p), WB, IHC(f)

Clonality: Monoclonal

Host: Rat

Purification: Supernatant

Reactivity: Human, Bovine

COMP – cartilage oligomeric matrix protein – is a prominent multidomain glycoprotein of cartilage, accounting for up to 1% of the wet weight of articular tissues and having an approximate Mr of 97 kDa. COMP may also be found in tendon, bone (i.e. osteoblasts), ligament, certain smooth muscles and synovium. In the ECM COMP is present in a pentameric, disulfide-bonded complex with a Mr of about 550 kDa. Although the function of COMP is not completely elucidated, it appears to mediate chondrocyte attachment via integrins and to stabilize the articular cartilage ECM via specific cation-dependent interactions with collagen types II and IX, aggrecan, fibronectin, and ECM protein 1. In addition, mutations in the human COMP gene have been linked to the development of pseudoachondroplasia and multiple epiphyseal dysplasia, which are autosomal-dominant forms of short-limb dwarfism. In chondrocytes of these patients, COMP remains frequently entrapped in intracellular vesicles. COMP is a substrate for a variety of ECM degrading enzymes, including MMP-1, MMP-13, MMP-19, MMP20 and ADAMTS-4, -7 and -12. Fragments of COMP have been detected in the diseased cartilage, synovial fluid, and serum of patients with knee injuries, post-traumatic and primary osteoarthritis and rheumatoid arthritis and have proposed to be diagnostic/prognostic of degenerative cartilage diseases.

References:
1) Di Cesare, et.al., 2000. Expression of cartilage oligomeric matrix protein (COMP) by embryonic and adult osteoblasts. J. Orthopaed. Res. 18, 713-720.
2) Di Cesare, et. Al., 2002. Matrix-matrix interactions of cartilage oligomeric matrix protein and fibronectin. Matrix Biol. 21, 461-465.

Application: WB, ELISA, Immuno-inhibition, IF, ICC

Clonality: Monoclonal

Host: Mouse

Purification: IgG

Reactivity: Human

Nucleotide excision repair (NER) is a major repair system for removing a variety of DNA lesions including UV-induced cyclobutane pyrimidine dimers and (6-4) photoproducts as well as chemically-induced bulky base adducts. Defects in the NER system give rise to xeroderma pigmentosum (XP), an autosomal recessive disease characterized by a predisposition to skin cancer and in some cases neurological abnormalities. The early process of human NER, from damage recognition to dual incision (removal of damage-containing oligonucleotides), is accomplished by six core NER factors, XPC-RAD23B, TFIIH, XPA, RPA, XPF-ERCC1 and XPG.

XP (Xeroderma pigmentosum) is an autosomal recessive human disease characterized by hypersensitivity to sunlight and a high incidence of skin cancer on sun-exposed skin (1). Cells from XP patients are hypersensitive to killing by UV irradiation because of a defect in nucleotide excision repair (NER). XP is classified into seven complementation groups (A-G) and a variant form (1). XPA shows the most severe symptoms. Products encoded by the XP genes function in repairing UV-induced cyclobutane pyrimidine dimmer and (6-4) photoproducts as well as chemically induced variety of DNA lesions (1). XPA protein consists of 273 amino acids and forms a complex with many proteins such as RPA, ERCC1, TFIIH, XAB1, and XAB2, which play roles in early steps of NER.

The hybridoma 5F12 was constructed by Prof. K. Tanaka’s group who first cloned the XPA gene (2, 3).

References:
1) Friedberg E C et. al., DNA Repair and Mutagenesis 2nd ed., ASM Press (2006).
2) Saijo M et al “Inhibition of nucleotide excision repair by anti-XPA monoclonal antibodies which interefere with
binding to RPA, ERCC1, and TFIIH” Biochem Biophys Res Comm 321:815-822 (2004). PMID: 15358100
3) Tanaka K et al “Analysis of a human DNA excision repair gene involved in group A xeroderma pigmentosum
and containing a zinc-finger domain” Nature 348:73 -76 (1990). PMID: 2234061

Application: IF, IHC(p), WB

Clonality: Polyclonal

Host: Rabbit

Purification: Purified – Affinity

Reactivity: Bovine, Human, Rat

Background

Neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.

Lens proteins consist almost entirely of crystallins (about 95%). Crystallins are also found in vertebrate skeletal muscle tissue. In the lens, their structural function is to assist in maintaining the proper refractive index of the lens. The mammalian lens contains 3 major classes of crystallins: alpha, beta, and gamma. Alpha-crystallin is the largest of the crystallins and is composed of 2 primary gene products, alpha-A and alpha-B. There are at least 5 different proteins comprising the beta-crystallins. The gamma-crystallins are monomeric, but there are at least 5 gamma crystallins identified in bovine and rat lens.
Alpha-Crystallin comprises 40% of total lens protein composition. In addition to maintaining proper refractive index, it also functions in a chaperone like manner by preventing the formation of aggregates possibly leading to cataract formation. It is believed that the phosphorylated states of the alpha-crystallin occur in response to cellular stress and may serve a structural control function and play a role in protein maintenance. Alpha-B crystallin has been linked to Alexander and quotes disease where it accumulates in brain cells of those afflicted.

Applications

Western Blotting (WB):0.5 µg/ml
Immunofluorescence (IF):5 µg/ml
Immunohistochemistry (Paraffin) (IHC (P)): assay dependent

Product description

References
1) Ito H, Okamoto K, Nakayama H, Isobe T, Kato K. (1997) Phosphorylation of B-crystallin in response to various types of stress. J Biol Chem. 272, 29934-29941.
2) Kato K, Ito H, Kamei K, Inaguma Y, Iwamoto I, Saga S. (1998) Phosphorylation of B-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J Biol Chem. 273, 28346-28354.
3) Ito H, Iida K, Kamei K, Iwamoto I, Inaguma Y, Kato K. (1999) B-crystallin in rat lens is phosphorylated at an early postnatal age. FEBS Lett. 446, 269-272.

Application: WB, IHC

Clonality: Monoclonal

Host: Mouse

Purification: Ascities

Reactivity: Bovine

Application: FC, IP

Clonality: Monoclonal

Host: Mouse

Purification: IgG

Reactivity: Human

Anti-IL-13Rα1 domain antibody is a mouse monoclonal antibody which obtained from the immunization with purified, silkworm-derived, recombinant human IL-13Rα1 domain. This antibody can be used for the detection of human IL-13Rα1 domain by immunoprecipitation and flow cytometry.