作者： 上海金畔生物

Cosmo Bio抗体,Cosmo Bio,Anti Proprotein Convertase Subtilisin/Kexin Type 6 (PACE4) – Propeptide pAb (Rabbit, Antiserum),CAC-SK-T01-002

Application: WB, IHC, IP, ELISA

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Human

PACE4A is a member of the mammalian subtilisin-like proprotein convertase family which is responsible for the proteolytic activation of precursors into their biologically active forms. Previously we reported that the maturation of proPACE4A occurs via a intramolecular autoactivation and cleavage of the propeptide is a rate-limiting step for the secretion of PACE4A (Nagahama et al., FEBS Lett. (1998) 434, 155–159). Although PACE4A is a putative secretory enzyme, it matures and is secreted much slower than general secretory proteins. In this study, we investigated the molecular mechanism underlying this slow maturation. The deletion of 25 amino acids at the carboxy terminus is sufficient for a marked acceleration in both the maturation and secretion of PACE4A. The carboxyl-truncated proPACE4A existed only as a monomer-sized form in the endoplasmic reticulum, whereas the wild type of proPACE4A existed in larger forms. Further, the fusion construct of yellow fluorescent protein and the carboxy-terminal sequence of PACE4A associated with the proPACE4A moiety and inhibited maturation. Thus, the carboxy terminus of PACE4A functions as a potent autoinhibitor of its activation, resulting in the retention of proPACE4A in the endoplasmic reticulum. These findings indicate that PACE4A activity is highly controlled by a unique system at post-translational level. [from: Taniguchi T., Kuroda R., Sakurai K., Nagahama M., Wada I., Tsuji A., Matsuda Y. A Critical Role for the Carboxy Terminal Region of the Proprotein Convertase, PACE4A, in the Regulation of Its Autocatalytic Activation Coupled with Secretion (2002) Biochemical and Biophysical Research Communications 290(2) 878-884.]

Source: Professor Akihiko Tsuji, Faculty of Engineering, Tokushima University

Cosmo Bio抗体,Cosmo Bio,Anti 20S Proteasome Subunit Alpha Type-4 mAb (Clone GC3β),CAC-SZU-PS-M02

Application: WB

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Plant, Fish, Rat, Human, Yeast, Frog

Regulating protein stability and turnover is a key task in the cell. Besides lysosomes, ubiquitin‐mediated proteasomal degradation comprises the major proteolytic pathway in eukaryotes. Proteins destined for degradation by the proteasome are conjugated by a ‘tag’, a ubiquitin chain to a lysine, through an extensively regulated enzymatic cascade. The ubiquitylated proteins are subsequently targeted for degradation by the 26S proteasome, the major proteolytic machinery for ubiquitylated proteins in the cell. Ubiquitylation can be considered as another covalent post‐translational modification and signal, comparable to acetylation, glycosylation, methylation, and phosphorylation. However, ubiquitylation has multiple roles in addition to targeting proteins for degradation. Depending on the number of ubiquitin moieties and the linkages made, ubiquitin also plays an important role in DNA repair, protein sorting and virus budding. Unregulated degradation of proteins, or abnormally stable proteins, interfere with several regulatory pathways, and the ubiquitin‐proteasome pathway is affected in a number of diseases, such as neurodegenerative diseases, cellular atrophies and malignancies. Therefore, dissecting the ubiquitin‐proteasome pathway and identifying proteins involved in conjunction with the signals required for specific degradation of certain substrates, would help in developing novel therapeutic approaches to treat diseases where the ubiquitin‐proteasome pathway is impaired. [from: Roos‐Mattjus P. and Sistonen L. The ubiquitin‐proteasome pathway (2009) Annals of Medicine 36(4): 285-295]

The 26S proteasome is an essential component of the ubiquitin-proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. It is composed of a 20S proteasome catalytic core and regulatory particles at either end. The subunits of the 20S proteasome are classified into two families, α and β. In eukaryotes, the 20S proteasome contains seven α-type subunits and seven β-type subunits. The fourteen subunits are arranged in four rings of seven and form an α7β7β7α7 structure. This antibody recognizes the α4 subunit of the 20S proteasome from all organisms tested from yeast to human.

References:
1) Tokumoto, M., Horiguchi, R., Nagahama, Y., Tokumoto, T. 1999. Identification of the Xenopus 20S proteasome alpha4 subunit which is modified in the meiotic cell cycle. Gene 239, 301-308. PubMed: 10548731
2) Tokumoto, M., Horiguchi, R., Nagahama, Y., Ishikawa, K., Tokumoto, T. 2000. Two proteins, a goldfish 20S proteasome subunit and the protein interacting with 26S proteasome, change in the meiotic cell cycle. Eur J Biochem 267, 97-103. PubMed: 10601855

Cosmo Bio抗体,Cosmo Bio,Anti Serpin B3 (SCCA1/T4-A) mAb (Clone SS6C),CAC-SU-IZ-M08

Application: IP, ELISA

Clonality: Monoclonal

Host: Rat

Purification: Ig-PG

Reactivity: Human

Squamous cell carcinoma antigen (SCCA) is a member of the ovalbumin family of serine proteinase inhibitors. The protein was isolated from a metastatic cervical squamous cell carcinoma by Kato and Torigoe (1977). SCCA is detected in the superficial and intermediate layers of normal squamous epithelium, whereas the mRNA is detected in the basal and sub-basal levels. The clinical import of SCCA has been as a circulating tumor marker for squamous cell carcinoma, especially those of the cervix, head and neck, lung, and esophagus. Many clinical studies of cervical squamous cell carcinoma show that the percentage of patients with elevated circulating levels of SCCA increases from approximately 12% at stage 0 to more than 90% at stage IV. Levels fall after tumor resection and rise in approximately 90% of the patients with recurrent disease. Similar trends occur in the other types of squamous cell carcinoma, with a maximum sensitivity of approximately 60% for lung, 50% for esophageal, and 55% for head and neck tumors. The neutral form of SCCA (SCCA1, or SERPINB3) is detected in the cytoplasm of normal and some malignant squamous cells, whereas the acidic form (SCCA2, or SERPINB4) is expressed primarily in malignant cells and is the major form found in the plasma of cancer patients. Thus, the appearance of the acidic fraction of SCCA is correlated with more aggressive tumors (summary by Schneider et al., 1995). Gene expression microarray profiling analysis has identified squamous cell cancer antigen (SCCA) as an IL-13 inflammation-induced gene in tracheal epithelial cells and keratinocytes. SCCA expression is increased in asthmatic bronchiale and atopic dermatitis skin. Two isoforms of SCCA are known: SCCA1 and SCCA2.

Source: Professor Kenji Dehara, Professor of Molecular Life Science, Faculty of Medicine, Saga University.

References:
1) The usefulness of combined measurements of squamous cell carcinoma antigens 1 and 2 in diagnosing atopic dermatitis. Shoichiro Ohta, et al. 2012. Ann Clin Biochem. 49: 277-284.
2) Characterization of novel squamous cell carcinoma antigen-related molecules in mice. Y. Sakata, et al. 2004. Biochem Biophys Res Commun. 324(4):1340-1345.
3) The squamous cell carcinoma antigens as relevant biomarkers of atopic dermatitis. K. Mitsuishi, et al. 2005. Clin Exp Allergy 35:1327-1333.
4) Involvement of IL-32 in activation-induced cell death in T cells. Chiho Goda, et al. 2006. Int Immunol 18(2):233-240.

Cosmo Bio抗体,Cosmo Bio,Anti C9ORF72 (Poly-GA) pAb (Rabbit, Antiserum),CAC-TIP-C9-P01

Anti-C9ORF72 (Poly-GA) pAb — prepared from rabbits immunized with poly (GA)8 — recognizes poly (GA) dipeptide repeat proteins. Validated for ELISA and IHC(p), this antibody is useful for immunohistochemical and biochemical studies of C9ORF72 (Poly-GA) dipeptide species in diseased brains.

In 2011 hexanucleotide expansions in the C9ORF72 gene were identified in patients with frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). GGGGCC expansions are characterized pathologically by the presence of TDP-43 negative and p62 positive inclusions in granule cells of the cerebellum and in cells of the dentate gyrus and CA4 area of the hippocampus. It was reported that these inclusions included dipeptide repeat proteins, poly-GA, poly-GR and poly-GP, arising from a putative non-ATG initiated sense translation of the GGGGCC expansion. These antibodies are powerful tools for IHC analysis of neurodegenerative diseases.

Specifications

• Product type                primary antibody
• Immunogen                 poly (GA)8
• Raised in                     rabbit
• Source                         anti-serum
• Form                           liquid anti-serum with 0.1% NaN3 as a preservative
• Volume                       50 uL
• Label                           unlabeled
• Specificity                   poly (GA)8
• Cross reactivity           human
• Storage                        below -20°C. (below -70°C for prolonged storage). Aliquot to avoid cycles of freeze/thaw.

Recommended dilutions

• ELISA                                     1/500-1/2000
• Immunohistochemistry           1/500-1/2000
• Other applications have not been tested
• Optimal dilutions/ concentrations should be determined by the end user.

References

1. David MA Mann, et al. Dipeptide repeat proteins are present in the p62 positive inclusions in patients with frontotemporal lobar degeneration and motor neuron disease associated with expansions in C9ORF72. Acta Neuropathologica Communications (2013) 1:68. PMID 24252525
2. Tan RH, et al. Cerebellar neuronal loss in als cases with ATXN2 intermediate repeat expansions. Ann Neurol. 2015 Nov 24. doi: 10.1002/ana.24565. PMID:26599997
3. Davidson Y, et al. Neurodegeneration in Frontotemporal Lobar Degeneration and Motor Neuron Disease associated with expansions in C9orf72 is linked to TDP-43 pathology and not associated with aggregated forms of dipeptide repeat proteins. Neuropathol Appl Neurobiol. 2015 Nov 5. doi: 10.1111/nan.12292. PMID: 26538301
4. Baborie A, et al. Accumulation of dipeptide repeat proteins predates that of TDP-43 in frontotemporal lobar degeneration associated with hexanucleotide repeat expansions in C9ORF72 gene. Neuropathol Appl Neurobiol. 2015 Aug;41(5):601-12. doi: 10.1111/nan.12178. Epub 2015 Apr 30. PMID: 25185840
5. Davidson YS, et al. Brain distribution of dipeptide repeat proteins in frontotemporal lobar degeneration and motor neurone disease associated with expansions in C9ORF72. Acta Neuropathol Commun. 2014 Jun 20;2:70. doi: 10.1186/2051-5960-2-70. PMID: 24950788
6. Konno T, et al. C9ORF72 repeat-associated non-ATG-translated polypeptides are distributed independently of TDP-43 in a Japanese patient with c9ALS. Neuropathol Appl Neurobiol. 2014 Oct;40(6):783-8. doi: 10.1111/nan.12157. No abstract available. PMID: 24861677

Cosmo Bio抗体,Cosmo Bio,Anti Canine T-Cell Surface Glycoprotein CD3 Epsilon Chain (CD3E) mAb (Clone 1B9-7-1-1),CAC-ABS-070001

Application: WB

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Dog

Background
The CD3-epsilon polypeptide, which together with CD3-gamma, -delta and -zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. This complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. The genes encoding the epsilon, gamma and delta polypeptides are located in the same cluster on chromosome 11. The epsilon polypeptide plays an essential role in T-cell development.[7] [from: Wikipedia contributors. (2018, October 25). T-cell surface glycoprotein CD3 epsilon chain. In Wikipedia, The Free Encyclopedia. Retrieved 21:31, June 3, 2019]

Cosmo Bio抗体,Cosmo Bio,Anti Monocarboxylate transporter 2 (MCT2) pAb (Rabbit, Antiserum),CAC-YCU-M-MCT2A

Application: WB

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Mouse

A transport protein (variously referred to as a transmembrane pump, transporter, escort protein, acid transport protein, cation transport protein, or anion transport protein) is a protein that serves the function of moving other materials within an organism. Transport proteins are vital to the growth and life of all living things. There are several different kinds of transport proteins. Carrier proteins are proteins involved in the movement of ions, small molecules, or macromolecules, such as another protein, across a biological membrane.[1] Carrier proteins are integral membrane proteins; that is, they exist within and span the membrane across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion (i.e., passive transport) or active transport. These mechanisms of movement are known as carrier-mediated transport.[2] Each carrier protein is designed to recognize only one substance or one group of very similar substances. Research has correlated defects in specific carrier proteins with specific diseases.[3] A membrane transport protein (or simply transporter) is a membrane protein[4] that acts as such a carrier. [from: Wikipedia contributors. (2019, May 9). Transport protein. In Wikipedia, The Free Encyclopedia. Retrieved 18:43, June 6, 2019, from https://en.wikipedia.org/w/index.php?title=Transport_protein&oldid=896329420]

MCT2 is a proton-coupled monocarboxylate transporter is encoded in humans by the SLC16A7 gene.[5] It catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate and beta-hydroxybutyrate. It also functions as high-affinity pyruvate transporter. Both Northern blot analysis and inspection of the human expressed sequence tag (EST) database suggest relatively little expression of MCT2 in human tissues. As well, the sequence of MCT2 is far less conserved across species than that of MCT1 or MCT4 and there also appear to be considerable species differences in the tissue expression profile of this isoform. Of the four known mammalian lactate transporters (MCTs 1-4), MCT2 harbors the highest affinity for lactate.[6] In parallel, MCT2 gene transcription has been demonstrated to respond with high-sensitivity to hypoxia, intracellular pH, and, to lactate.[7] [from: Wikipedia contributors. (2019, April 20). Monocarboxylate transporter 2. In Wikipedia, The Free Encyclopedia. Retrieved 18:41, June 6, 2019, from https://en.wikipedia.org/w/index.php?title=Monocarboxylate_transporter_2&oldid=893305296]

References:
1) Watanabe-Kaneko K, et al. (2007) The synaptic scaffolding protein Delphilin interacts with monocarboxylate transporter 2. Neuroreport. 18(5):489-493.

Cosmo Bio抗体,Cosmo Bio,Anti DEP Domain-Containing Protein 1B (XTP1/XTP8) mAb (Clone 2191H11),CAC-PRPG-XTP-M01

Application: WB, IHC

Clonality: Monoclonal

Host: Mouse

Purification: Supernatant

Reactivity: Human

The RhoGAP family embraces a unique member named XTP1 (also referred to as DEPDC1B, BRCC3 or FLJ11252) and pairing with a homologue denoted SDP35 (also referred to as DEPDC1, DEP8, FLJ20354 or DEPDC1-V2). The structural-functional properties of XTP1 are still largely unknown, but its structural uniqueness resides in the presence of a domain showing homology with Dishwelled, i.e. the DEP domain (Dishwelled/Pleckstrin-like domain). The presence of this domain suggests that XTP1 might engage in more complex molecular interactions than those of other members of the family. Another peculiar feature of XTP1 is represented by its atypical GAP domain, which lacks the orthodox “Arg finger” catalytic motif essential for exerting canonical GAP function. Whereas most RhoGAP family members are either ubiquitously expressed throughout the body or are concentrated in discrete tissue/organs, XTP1 is remarkably poorly represented in most human adult tissues (also supported by evidence provided by the Comparative Cancer Genome Project database). XTP1 is de novo expressed upon neoplastic transformation and remains abundant in many cancer cell lines. Some observations in epithelial tumors suggest that it may act as a cell-cycle regulator.

Cosmo Bio抗体,Cosmo Bio,Anti Human Transmembrane Glycoprotein NMB (GPNMB) pAb (Rabbit, Purified Ig),CAC-ICA-TG1-RBP1

Application: FC, ELISA, IHC

Clonality: Polyclonal

Host: Rabbit

Purification: Ig-PA

Reactivity: Human

Lipid-laden macrophages may orchestrate pathology, an accepted notion for inborn lysosomal storage disorders (LSDs) and more recently for metabolic syndrome. The development of enzyme replacement therapy (ERT) for specific LSDs has led in the last decades to the identification of markers of lipid-laden macrophages. In LSDs characterized by foamy macrophages as storage cells, plasma GPNMB has been shown to accurately reflect disease burden. Moreover, GPNMB is also applicable in mouse models of LSDs like Gaucher disease and Niemann-Pick type C. GPNMB is also increased in several acquired diseases, such as metabolic syndrome and neurodegeneration. It therefore might be that these disease conditions share pathophysiological elements, in particular the accumulation of foamy, lysosomal stressed, macrophages. GPNMB is among the most upregulated proteins in lipid-laden macrophages. Nevertheless, at present its exact function in foamy macrophage remains largely enigmatic. Important unanswered questions concern the function(s) served by GPNMB, either the cellular membrane-bound or (extracellular) soluble isoforms, in lipid-laden macrophages and beyond. GPNMB is also expressed in melanocytes. GPNMB has been suggested to be involved in the delay of cell growth and regulation of metastasis. In recent years, Professor Hideaki Hara’s group at Gifu Pharmaceutical University, and others have shown that GPNMB expression is suppressed in mice that have developed amyotrophic lateral sclerosis (ALS), and tracking of GPNMB dynamics and function has been shown to be useful for ALS research.

Cosmo Bio抗体,Cosmo Bio,Anti Feline T-Cell Surface Glycoprotein CD3 Epsilon Chain (CD3E) mAb (Clone 5G-6-7-3),CAC-ABS-070002

Application: FC, ELISA, WB

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Cat

Background
The CD3-epsilon polypeptide, which together with CD3-gamma, -delta and -zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. This complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. The genes encoding the epsilon, gamma and delta polypeptides are located in the same cluster on chromosome 11. The epsilon polypeptide plays an essential role in T-cell development.[7] [from: Wikipedia contributors. (2018, October 25). T-cell surface glycoprotein CD3 epsilon chain. In Wikipedia, The Free Encyclopedia. Retrieved 21:31, June 3, 2019]

Cosmo Bio抗体,Cosmo Bio,Anti Androstenedione pAb (Rabbit, Antiserum),CAC-KZ-HS-P15

Application: ELISA, RIA

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Bovine, Human, Rat, Mouse, Chicken

Androstenedione, or 4-androstenedione (abbreviated as A4 or Δ4-dione), also known as androst-4-ene-3,17-dione, is an endogenous weak androgen steroid hormone and intermediate in the biosynthesis of estrone and of testosterone from dehydroepiandrosterone (DHEA). It is closely related to androstenediol (androst-5-ene-3β,17β-diol). Androstenedione is a precursor of testosterone and other androgens, as well as of estrogens like estrone, in the body. In addition to functioning as an endogenous prohormone, androstenedione also has weak androgenic activity in its own right. Androstenedione has been found to possess some estrogenic activity, similarly to other DHEA metabolites.[2] However, in contrast to androstenediol, its affinity for the estrogen receptors is very low, with less than 0.01% of the affinity of estradiol for both the ERα and ERβ.[3] [from: Wikipedia contributors. (2019, April 7). Androstenedione. In Wikipedia, The Free Encyclopedia. Retrieved 20:45, June 3, 2019, from https://en.wikipedia.org/w/index.php?title=Androstenedione&oldid=891404493]

Cosmo Bio抗体,Cosmo Bio,Anti Alpha Synuclein (Amino Acids 61-70) pAb (Rabbit, Antiserum),CAC-TIP-SN-P07

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

Cosmo Bio抗体,Cosmo Bio,Anti Ginsenoside Rb1 mAb (Clone 9G7),CAC-KYU-HT-M003

Application: ELISA, WB

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Within the fields of molecular biology and pharmacology, a small molecule is a low molecular weight (< 900 daltons) organic compound that may regulate a biological process, with a size on the order of 1 nm. Most drugs are small molecules. Larger structures such as nucleic acids and proteins, and many polysaccharides are not small molecules, although their constituent monomers (ribo- or deoxyribonucleotides, amino acids, and monosaccharides, respectively) are often considered small molecules. Small molecules may be used as research tools to probe biological function as well as leads in the development of new therapeutic agents. Some can inhibit a specific function of a protein or disrupt protein–protein interactions.

Pharmacology usually restricts the term “small molecule” to molecules that bind specific biological macromolecules and act as an effector, altering the activity or function of the target. Small molecules can have a variety of biological functions or applications, serving as cell signaling molecules, drugs in medicine, pesticides in farming, and in many other roles. These compounds can be natural (such as secondary metabolites) or artificial (such as antiviral drugs); they may have a beneficial effect against a disease (such as drugs) or may be detrimental (such as teratogens and carcinogens). [from: Wikipedia contributors. (2019, April 6). Small molecule. In Wikipedia, The Free Encyclopedia. Retrieved 19:49, May 29, 2019, from https://en.wikipedia.org/w/index.php?title=Small_molecule&oldid=891243496]

Ginsenoside Rb1 is a saponin isolated from Panax ginseng.

References:
1) Tanaka H. et al., Formation of monoclonal antibody against a major ginseng component, ginsenoside Rb1 and its characterization, Cytotechnology, 29,115, 1999. PMID:22359060.
2) Fukuda N, Tanaka H, Shoyama Y. (2001) Double staining of ginsenosides by Western blotting using anti-ginsenoside Rb1 and Rg1 monoclonal antibodies. Biol Pharm Bull. 24(10):1157-60. PMID:11642323.

Cosmo Bio抗体,Cosmo Bio,Anti-Latency-Associated Peptide (LAP) Plasma Kallikrein Degradation Fragment R58 mAb (Clone 18F9-16),CAC-RIK-MA-R58

Background
Anti-Latency-Associated Peptide (LAP) Plasma Kallikrein Degradation Fragment R58-specific mAb 18F9-16 was cloned from mice immunized with R58 peptide [CGQILSKLR]. 18F9-16 recognizes the C-terminus cut end of LAP degradation product (LAP-D) R58 produced when latent TGF-β is digested with Plasma Kallikrein. 18F9-16 is validated for IHC and IF.

TGF-β is produced as a pro-protein latent complex in which a 25 kDa active TGF-β fragment is trapped by an N-terminal pro-peptide called Latency Associated Protein (LAP). Active TGF-β is released from the latent complex in a process called the TGF-β activation reaction involving a conformational change induced by binding of the latent complex to cell adhesion proteins such as thrombospondin and integrins, and/or by being cleaved by serine proteases, cysteine proteases, and MMPs in an organ and context-depending manner.

Kojima and his colleagues in the Cellular Molecular Pathology Research Unit (currently, Center for Integrative Medical Sciences, Liver Cancer Prevention Research Unit), RIKEN, Japan focused on the role of serine proteases plasmin and plasma kallikrein in the release and activation of TGF-β and its involvement in liver diseases. They showed that plasmin and plasma kallikrein cleave, respectively, at Lys⁵⁶-Leu⁵⁷ and Arg⁵⁸-Leu⁵⁹ within the LAP portion of the latent TGF-β1 molecule. The anti-TGF-β1 LAP-degradate (LAP-D) antibodies are useful for investigating the molecular mechanism of TGF-β activation and its related diseases, including liver fibrosis/cirrhosis and liver degeneration.

Applications

• Immunohistochemistry (IHC)            10 μg/mL
• Optimal dilutions/concentrations should be determined by the end user.

Specifications

• Host Species               mouse
• Form                           liquid, PBS (pH 7.4), 0.05% NaN3
• Volume                       100 μg (1 mg/mL)
• Specificity                   recognizes C-terminus cut end of LAP degradation product (LAP-D) R58 when latent TGF-β is digested with Plasma Kallikrein (PLK).
• Antigen                       R58 peptide [CGQILSKLR]
• Clonality                     monoclonal (clone # 18F9-16)
• Isotype                        IgG3
• Purification                 purified by affinity column (Protein A) from serum-free cell culture medium
• Conjugation                none
• Storage condition        store below -20°C (below -70°C for prolonged storage) Aliquot to avoid freeze/thaw cycles.

Product Description

References

• (1)LAP degradation product reflects plasma kallikrein-dependent TGF-β activation in patients with hepatic fibrosis.
  Hara M, Kirita A, Kondo W, Matsuura T, Nagatsuma K, Dohmae N, Ogawa S, Imajoh-Ohmi S, Friedman SL, Rifkin DB, Kojima S.
  Springerplus. 2014 May 1;3:221. doi: 10.1186/2193-1801-3-221. eCollection 2014. PMID: 24877031
• (2)L(59) TGF-β LAP degradation products serve as a promising blood biomarker for liver fibrogenesis in mice.
  Hara M, Inoue I, Yamazaki Y, Kirita A, Matsuura T, Friedman SL, Rifkin DB, Kojima S.
  Fibrogenesis Tissue Repair. 2015 Sep 15;8:17. doi: 10.1186/s13069-015-0034-9. eCollection 2015. PMID: 26379781

Cosmo Bio抗体,Cosmo Bio,Anti CD63 Antigen (LAMP-3/Tspan-30) (Clone 8A12, TF2SW Labeled),CAC-SHI-EXO-M02-TF2

Application: FC

Clonality: Monoclonal

Conjugation: Tide Fluor™ 2SW

Host: Mouse

Purification: Ig-PG

Reactivity: Human

Click here for more information and to see all exosome related products from Cosmo Bio USA.

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.

Cosmo Bio抗体,Cosmo Bio,Anti CD81 Antigen (TAPA-1/Tspan-28) mAb (Clone 12C4),CAC-SHI-EXO-M03-50

Application: IP, WB

Clonality: Monoclonal

Host: Mouse

Purification: Ig-PG

Reactivity: Bovine, Human

Click here for more information and to see all exosome related products from Cosmo Bio USA.

CD81 (TAPA-1) is a cell surface protein which belongs to the tetraspanin superfamily. CD81 is identified as a component of the B lymphocyte receptor (BCR) and as a receptor for the Hepatitis C Virus. 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) Takahashi A et al., Nat Commun. 2017 May 16;8:15287. doi: 10.1038/ncomms15287.
2) M Somiya et al., J Extracell Vesicles. 2018 Feb 21;7(1):1440132. doi:10.1080/20013078.2018.1440132. eCollection 2018.

Cosmo Bio抗体,Cosmo Bio,Anti Human/Rat/Mouse Transmembrane Glycoprotein NMB (GPNMB) pAb (Rabbit, Purified Ig),CAC-ICA-TG1-RBP3

Application: FC, ELISA, IHC

Clonality: Polyclonal

Host: Rabbit

Purification: Ig-PA

Reactivity: Mouse, Rat, Human

Lipid-laden macrophages may orchestrate pathology, an accepted notion for inborn lysosomal storage disorders (LSDs) and more recently for metabolic syndrome. The development of enzyme replacement therapy (ERT) for specific LSDs has led in the last decades to the identification of markers of lipid-laden macrophages. In LSDs characterized by foamy macrophages as storage cells, plasma GPNMB has been shown to accurately reflect disease burden. Moreover, GPNMB is also applicable in mouse models of LSDs like Gaucher disease and Niemann-Pick type C. GPNMB is also increased in several acquired diseases, such as metabolic syndrome and neurodegeneration. It therefore might be that these disease conditions share pathophysiological elements, in particular the accumulation of foamy, lysosomal stressed, macrophages. GPNMB is among the most upregulated proteins in lipid-laden macrophages. Nevertheless, at present its exact function in foamy macrophage remains largely enigmatic. Important unanswered questions concern the function(s) served by GPNMB, either the cellular membrane-bound or (extracellular) soluble isoforms, in lipid-laden macrophages and beyond. GPNMB is also expressed in melanocytes. GPNMB has been suggested to be involved in the delay of cell growth and regulation of metastasis. In recent years, Professor Hideaki Hara’s group at Gifu Pharmaceutical University, and others have shown that GPNMB expression is suppressed in mice that have developed amyotrophic lateral sclerosis (ALS), and tracking of GPNMB dynamics and function has been shown to be useful for ALS research.

Cosmo Bio抗体,Cosmo Bio,Anti TAR DNA-Binding Protein 43 (TDP43), phospho Ser410 pAb (Rabbit, Antiserum),CAC-TIP-PTD-P04

Anti-TAR DNA-Binding Protein 43 (TDP-43), phospho Ser410 pAb was prepared from rabbits immunized with phospho-peptide [CMDSKSS(p)GWGM]. This pAb recognizes human TDP-43 phosphorylated on serine 410 and is validated for western blot, ELISA and IHC(f) analyses of TDP-43 proteinopathy.

TDP-43, a heterogeneous nuclear ribonucleoprotein, was identified as a component of ubiquitin-positive and tau-negative inclusions observed in cases of frontotemporal lobar degeneration (FTLD-U) and amyotrophic lateral sclerosis (ALS). Immunochemical analyses using antibodies generated against phospho- and non-phosphopeptides of human TDP-43 revealed that abnormally phosphorylated full-length TDP-43 (45 kDa), C-terminal fragments (~25 kDa) and smearing substances are deposited as intracellular inclusions in affected regions of FTLD-U and ALS cases. This antibody is a powerful tool for biochemical and immunohistochemical analyses of neurodegenerative diseases and for evaluation of cellular or animal models of TDP-43 proteinopathy.

Specifications

• Product type                primary antibody
• Immunogen                 CMDSKSS(p)GWGM, S(p): phosphoserine 410
• Raised in                     rabbit
• Source                         serum
• Form                           liquid antiserum with 0.05% NaN3 as a preservative
• Volume                       100 uL
• Label                           unlabeled
• Specificity                   phospho-TDP-43
• Cross reactivity           human
• Storage                        below -20°C and below -70°C for prolonged storage; aliquot to avoid freeze/thaw cycles.

Recommended dilutions

• Western blotting: 1/1000-1/3000
• Immunohistochemistry: 1/1000-1/5000
• ELISA: 1/1000-1/5000
• Other applications not tested
• Optimal dilutions/concentrations should be determined by end user

References

1. Hasegawa M, Arai T, Nonaka T, et al. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol. 2008;64(1):60–70. doi:10.1002/ana.21425

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Cosmo Bio抗体,Cosmo Bio,Anti Aggrecan (ACAN) mAb (Clone 5D3),CAC-PRPG-AG-M02

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.

Cosmo Bio抗体,Cosmo Bio,Anti Integrin Alpha-6 (VLA-6) mAb (Clone 537D5),CAC-PRPG-ITG-M01

Application: ICC, WB, FC, IHC(f), IF

Clonality: Monoclonal

Host: Mouse

Purification: Ascities

Reactivity: Human

Integrins are conserved, cation-dependent transmembrane receptors essential for cell survival and growth. They are comprised of α and β subunits that are differentially involved in ligand binding and connection with the cytoskeleton. They link cells to the extracellular matrix (ECM) and to cell surface-bound adhesion molecules, such as to allow cells to properly organize within tissues in relation to underlying and/or surrounding matrices. Thus, in epithelia and vasculature integrins are critical in structuring the intricate junctional complexes with underlying basement membranes, whereas in connective tissues they allow cells to form stable attachments (i.e. focal adhesions) with their surrounding interstitial matrices and rapidly convert (bidirectionally) from stationary to motile phenotypes. Integrins not engaged in ligand binding are generally dispersed on the surface of cells but tend to form microclusters. Upon ligand engagement they reorganize to form larger clusters that permit the stabilization of cell-ECM or cell-cell interactions.

Simultaneously, through phosphorylation of the cytoplasmic portion of the β subunit, integrins associate with key cytoskeletal adapter proteins, such as vinculin, talin, paxillin, tensin and FAK to activate complex signal transduction pathways converging with those elicited by growth factor receptors and other receptors for soluble and membrane-bound signal molecules. This results in the activation of the cell cycle, cell differentiation programs and/or the acquisition of motile properties. Conversely, loss of integrin binding to the matrix causes a type of programmed cell death known as anoikis. There are more than 15 α subunits and 8 β subunits, which pair with each other in different combinations to generate a repertoire of over 20 different integrin receptors. These may be selective, binding one or two ligands or promiscuous, binding multiple ligands. Similarly, the same ECM component may be recognized by one individual integrin receptor or multiple receptors. Integrin expression is frequently altered in pathological conditions and mutations in the INTG genes are associated with inheritable diseases. In cancer, integrins are fundamental in conferring a more aggressive behavior to malignant cells and are therefore considered attractive therapeutic targets. However, thus far, only one anti-integrin drug is registered for clinical application and its use is for the treatment of neurological rather neoplastic diseases.

The α6 integrin subunit pairs with two distinct β subunits, β1 and β4, and with the latter one it forms a unique integrin receptor that is essential for the assembly and maintenance of hemidesmosomes. There are a total 8 different alternatively-spliced α6 isoforms known which show a diverse tissue distribution, i.e. isoforms containing segment X1 are ubiquitously expressed, whereas isoforms containing segment X1X2 are expressed in heart, kidney, placenta, colon, duodenum, myoblasts and myotubes. Similarly, in some tissues, isoforms containing cytoplasmic segment A and isoforms containing segment B are detected while in others, only isoforms containing one cytoplasmic segment are found.