TQ1 CPG
AAT代理,TQ1 CPG,微信同号 18301939375，部分现货，欢迎来电咨询
上海金畔生物科技有限公司代理AAT Bioquest荧光染料全线产品，欢迎访问AAT Bioquest荧光染料官网了解更多信息。
AAT代理,TQ1 CPG
AAT代理,TQ1 CPG,微信同号 18301939375，部分现货，欢迎来电咨询
上海金畔生物科技有限公司代理AAT Bioquest荧光染料全线产品，欢迎访问AAT Bioquest荧光染料官网了解更多信息。
标签： CPG
AAT代理,TQ1 CPG,微信同号 18301939375，部分现货，欢迎来电咨询
上海金畔生物科技有限公司代理AAT Bioquest荧光染料全线产品，欢迎访问AAT Bioquest荧光染料官网了解更多信息。
lumiprobe -Universal CPG type II, 1000A
- Products
- DNA
- CPG solid supports
- Universal CPG type II, 1000A
Universal CPG type II, 1000A
| Cat. # | Quantity | Price | Lead time | |
|---|---|---|---|---|
| 2923-1g | 1 g | 45.00$
|
||
| 2923-10g | 10 g | 410.00$
|
The Universal CPG type II, 1000A is one of universal supports used to immobilize nucleosides for synthesizing oligonucleotides and to increase rate of dephosphorylation of the 3′ end oligonucleotide during deblocking.
For the cleavage from the support and oligonucleotide deprotection anhydrous ammonia gas-phase, ammonium hydroxide/methylamine mixture and other basic reagents can be used in a short time. The Universal CPG type II, 1000A is suitable for use in harsh conditions and makes cleavage and deprotection faster compared to universal supports. Pore size of 1000 Å is recommended for the synthesis of oligonucleotides up to 120 bases.
Usage
Coupling: Standard conditions for universal CPG.
Deprotection: 2 hours at 80 °C or 8 hours at 55 °C using concentrated ammonia; 15 minutes at 65 °C using AMA mixture, ammonium hydroxide – 40% methylamine (1:1).
Customers also purchased with this product
DusQ2 CPG 1000
Controlled pore glass (CPG) 1000 modified support for the synthesis of oligonucleotides with DusQ2 quencher at the 3’ end. Compatible with standard deblocking conditions.
Controlled pore glass (CPG) 1000 solid support for synthesis of oligonucleotides with 3’-terminal DusQ1 quencher. Compatible with standard deblocking conditions.
Oligo synthesis details
| Pore size, Å: | 1000 |
| Typical loading, umol/g: | 50−95 |
| Coupling conditions: | standard coupling, identical to normal nucleobases |
| Cleavage conditions: | ammonium hydroxide 2 hours at 80 °C or 8 hours at 55 °C; AMA mixture, ammonium hydroxide – 40% methylamine (1:1), 15 minutes at 65 °C |
| Deprotection conditions: | identical to protected nucleobases |
The count of items is incorrect. 
lumiprobe – DusQ3 CPG 500,CPG solid supports,lumiprobe代理
- Products
- DNA
- CPG solid supports
- DusQ3 CPG 500
DusQ3 CPG 500
CPG (controlled pore glass) solid supports for oligonucleotide synthesis
| Cat. # | Quantity | Price | Lead time | |
|---|---|---|---|---|
| 1618-1g | 1 g | 990.00$ | 21 days |
DusQ3 is a dark quencher for far red and near infrared fluorophores, especially suitable for Cyanine5.5.
The dye can be attached to 3′-terminus of oligonucleotides by means of automated solid phase synthesis using this support. The dye is sensitive to nucleophilic reagents, and therefore must be carefully deprotected. We recommend the use of ultramild, phenoxyacetyl protected monomers. As an alternative, post-synthetic labeling using NHS ester of the quencher can be used.
Customers also purchased with this product
DusQ1 CPG 500
Controlled pore glass (CPG) 500 solid support for synthesis of oligonucleotides with 3’-terminal DusQ1 quencher. Compatible with standard deblocking conditions.
DusQ2 CPG 500
Controlled pore glass (CPG) 500 modified support for the synthesis of oligonucleotides with DusQ2 quencher at the 3’ end. Compatible with standard deblocking conditions.
| Appearance: | dark blue beads |
| Quality control: | 1H NMR of bound reagent, coupling testing with HPLC-MS |
| Storage conditions: | 24 months after receival at -20°C in the dark. Transportation: at room temperature for up to 3 weeks. Desiccate. Avoid prolonged exposure to light. |
| MSDS: | Download |
| Product specifications |
Oligo synthesis details
| Pore size, Å: | 500 |
| Typical loading, umol/g: | 50-80 |
| Coupling conditions: | standard, ultramild phosphoramidites |
| Cleavage conditions: | 2 h / rt, 30% aq. ammonia (ultramild protective groups) |
lumiprobe -Universal CPG type I, 500A
- Products
- DNA
- CPG solid supports
- Universal CPG type I, 500A
Universal CPG type I, 500A
| Cat. # | Quantity | Price | Lead time | |
|---|---|---|---|---|
| 2646-1g | 1 g | 39.00$
|
||
| 2646-10g | 10 g | 351.00$
|
The Universal CPG type I, 500A is one of universal supports used to immobilize nucleosides for high-throughput synthesizing oligonucleotides.
The cleavage from the support is followed by deprotection using anhydrous methylamine gas, ammonium hydroxide/methylamine mixture and other basic reagents. Universal support CPG type I is suitable for relatively aggressive environment treatment. Pore size of 500 Å is recommended for the synthesis of oligonucleotides up to 50 bases.
Usage
Coupling: Standard conditions for universal CPG.
Deprotection: 8 hours at 80 °C using ammonium hydroxide or 17 hours at 55 °C; 3 hours at 80 °C using AMA mixture, ammonium hydroxide – 40% methylamine (1:1) or 8 hours at 55 °C using 40% methylamine or 30 minutes at 80 °C; 3 hours at 55 °C; 17 hours at room temperature using 0.4M NaOH in methanol – water (4:1).
Customers also purchased with this product
Oligo synthesis details
| Pore size, Å: | 500 |
| Typical loading, umol/g: | 50−95 |
| Coupling conditions: | standard coupling, identical to normal nucleobases |
| Cleavage conditions: | AMA mixture, ammonium hydroxide – 40% methylamine (1:1), 3 hours at 80 °C |
| Deprotection conditions: | identical to protected nucleobases |
The count of items is incorrect.
ProSpec-CTGF Human
- Description
Catalogue number
CYT-541
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF , Nov , WISP-1, 2 and 3 . The CCN genes encode secreted proteins associated with the Extracellular Matrix and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the IGFBPs.
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand’s factor and mucins. Sequence similarities to binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Description
CTGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.2 kDa.
The CTGF is purified by proprietary chromatographic techniques.
The CTGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
CTGF was Lyophilized from a sterile filtered aqueous solution containing 0.1% Trifluoroacetic Acid .
Solubility
It is recommended to reconstitute the lyophilized CTGF in sterile 18MΩcm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized CTGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTGF should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein .
Please prevent freeze-thaw cycles.
Purity
Purity of CTGF is greater than 90% as determined by -PAGE.
Biological Activity
Determined by the dose-dependent stimulation of the proliferation of HUVEC cells. The expected ED50 for this effect is 1-2µg/ml, corresponding to a specific activity of 500-1000units/mg.
Amino acid sequence
MGKKCIRTPK ISKPIKFELS GCTSMKTYRA KFCGVCTDGR CCTPHRTTTL PVEFKCPDGE VMKKNMMFIK TCACHYNCPG DNDIFESLYY RKMYGDMA.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Related Products
-
CTGF Human
-
CTGF Human, HEK
-
CTGF Human, His
-
CTGF Antibody
-
CTGF Mouse
-
CTGF Human
ProSpec-CTGF Human, HEK
- Description
Catalogue number
CYT-687
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.
Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF , Nov , WISP-1, 2 and 3 . The CCN genes encode secreted proteins associated with the Extracellular Matrix and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand’s factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand’s factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Description
The CTGF Human Recombinant produced in HEK293 cells, is 36kDa protein containing a total of 329 amino acid residues including a C-terminal 6×His tag.
Source
HEK293 cells.
Physical Appearance
Filtered colorless solution.
Formulation
CTGF filtered solution in 0.1M Citrate buffer pH 4.7 and 20% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
Amino acid sequence
QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.
Purity
Greater than 90.0% as determined by -PAGE.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Related Products
-
CTGF Human
-
CTGF Human
-
CTGF Human, His
-
CTGF Antibody
-
CTGF Mouse
-
CTGF Human
ProSpec-CTGF Human, His
- Description
Catalogue number
CYT-438
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF , Nov , WISP-1, 2 and 3 . The CCN genes encode secreted proteins associated with the Extracellular Matrix and cell membrane. CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes. The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion. Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand’s factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy. In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells. CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes. The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion. Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand’s factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy. In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells. CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Description
CTGF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids and having a molecular mass of 37.7kDa.
The CTGF is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
The CTGF is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered clear solution.
Formulation
CTGF protein is supplied in 20mM Tris-HCl, pH-8 and 10% Glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
Purity
Greater than 85.0% as determined by Analysis by -PAGE.
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Related Products
-
CTGF Human, HEK
-
CTGF Human
-
CTGF Human
-
CTGF Antibody
-
CTGF Mouse
-
CTGF Human
ProSpec-CTGF Mouse
- Description
Catalogue number
CYT-1173
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Introduction
Connective Tissue Growth Factor is a part of the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 , CTGF, Nov , WISP-1, 2 and 3 . CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: tumorigenesis,fibrosis and vascular ailments. Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of 4 modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins .
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat .
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat , which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Description
CTGF Mouse Recombinant is a single, glycosylated polypeptide chain containing 329 amino acids and having a molecular mass of 36.2kDa . CTGF is fused to a 6 a.a His tag at C-terminal.
Source
HEK293
Physical Appearance
Filtered clear solution.
Formulation
CTGF protein solution is filtered in in 0.1M citrate buffer pH 4,7 and 20% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
Avoid multiple freeze-thaw cycles.
Purity
Greater than 95.0% as determined by -PAGE.
Amino acid sequence
QDCSAQCQCA AEAAPHCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCDFGS PANRKIGVCT AKDGAPCVFG GSVYRSGESF QSSCKYQCTC LDGAVGCVPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDRTAVG PALAAYRLED TFGPDPTMMR ANCLVQTTEW
SACSKTCGMG ISTRVTNDNT FCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKIAKPV KFELSGCTSV KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEIMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMAHHHHHH
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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CTGF Human
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CTGF Antibody
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CTGF Human
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CTGF Human, HEK
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CTGF Human, His
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CTGF Human
ProSpec-IGFBP6 (28-240) Human
- Description
Catalogue number
CYT-786
Synonyms
Insulin-like growth factor-binding protein 6, IBP-6, IGF-binding protein 6, IGFBP-6, IGFBP6, IBP6.
Introduction
IGFBP6 plays a role in lipoprotein assembly and dietary cholesterol absorption. in addition to its acyltransferase activity, it may act as a ligase. may provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.
Description
IGFBP6 Human Recombinant produced in E. coli is a single polypeptide chain containing 236 amino acids and having a molecular mass of 25.0kDa .
IGFBP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
IGFBP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
The IGFBP6 solution contains 20mM Tris-HCl buffer , 0.15M NaCl, 20% glycerol and 1mM DTT.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
Purity
Greater than 85% as determined by -PAGE.
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MGSRCPGCGQ GVQAGCPGGC VEEEDGGSPA EGCAEAEGCL RREGQECGVY TPNCAPGLQC HPPKDDEAPL RALLLGRGRC LPARAPAVAE ENPKESKPQA GTARPQDVNR RDQQRNPGTS TTPSQPNSAG VQDTEMGPCR RHLDSVLQQL QTEVYRGAQT LYVPNCDHRG FYRKRQCRSS QGQRRGPCWC VDRMGKSLPG SPDGNGSSSC PTGSSG.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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IGFBP6 Human
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IGFBP6 Mouse
ProSpec-IGFBP6 Mouse
- Description
Catalogue number
CYT-987
Synonyms
Insulin-like growth factor-binding protein 6, Igfbp6, IGFBP-6, IBP-6, IGF-binding protein 6, IGFBP-6, Igfbp-6.
Introduction
IGFBP6 plays a role in lipoprotein assembly and dietary cholesterol absorption. in addition to its acyltransferase activity, it may act as a ligase. may provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.
Description
IGFBP6 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 221 amino acids and having a molecular mass of 23.7kDa .
IGFBP6 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
IGFBP6 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
IGFBP6 protein solution contains Phosphate Buffered Saline and 40% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
Purity
Greater than 90.0% as determined by -PAGE.
Amino acid sequence
ALAGCPGCGA GMQTGCRGGC VEEEDAGSPA DGCTEAGGCL RREGQPCGVY SPKCAPGLQC QPRENEEAPL RALLIGQGRC QRARGPSEET TKESKPQGGA SRSRDTNHRD RQKNPRTSAA PIRPNPVQDS EMGPCRRHLD SVLQQLQTEV FRGGARGLYV PNCDLRGFYR KQQCRSSQGN RRGPCWCVDP MGQPLPVSPD GQGSTQCSAR SSGLEHHHHH H.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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IGFBP6 Human
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IGFBP6 Human
ProSpec-INSR Human
- Description
Catalogue number
CYT-777
Synonyms
Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.
Introduction
Insulin Receptor is a receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin to the insulin receptor stimulates glucose uptake. Once the precursor signal peptide is removed, the insulin receptor precursor is post-translationally cleaved into 2 chains which are covalently linked. Insulin binding initiates phosphorylation of several intracellular substrates, including, insulin receptor substrates , SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins function as docking proteins for other signaling proteins which contain Src-homology-2 domains that specifically recognize different phosphotyrosines residues, including the p85 regulatory subunit of PI3K and SHP2.
Description
Insulin Receptor Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 927 amino acids, having a molecular mass of 105.9kDa , though it migrates at approximately 160kDa on PAGE, the INSR is fused to a 2 a.a N-terminal linker, a 2 a.a C-terminal linker and fused to a 6 a.a His tag at C-Terminus.
The Human INSR is purified by proprietary chromatographic techniques.
The Human INSR is purified by proprietary chromatographic techniques.
Source
HEK 293.
Physical Appearance
Filtered White lyophilized powder.
Formulation
INSR was filtered and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. INSR is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Purity
Greater than 95.0% as determined by -PAGE.
Amino acid sequence
ASHLYPGEVC PGMDIRNNLT RLHELENCSV IEGHLQILLM FKTRPEDFRD LSFPKLIMIT DYLLLFRVYG LESLKDLFPN LTVIRGSRLF FNYALVIFEM VHLKELGLYN LMNITRGSVR IEKNNELCYL ATIDWSRILD SVEDNYIVLN KDDNEECGDI CPGTAKGKTN CPATVINGQF VERCWTHSHC QKVCPTICKS HGCTAEGLCC HSECLGNCSQ PDDPTKCVAC RNFYLDGRCV ETCPPPYYHF QDWRCVNFSF CQDLHHKCKN SRRQGCHQYV IHNNKCIPEC PSGYTMNSSN LLCTPCLGPC PKVCHLLEGE KTIDSVTSAQ ELRGCTVING SLIINIRGGN NLAAELEANL GLIEEISGYL KIRRSYALVS LSFFRKLRLI RGETLEIGNY SFYALDNQNL RQLWDWSKHN LTITQGKLFF HYNPKLCLSE IHKMEEVSGT KGRQERNDIA LKTNGDQASC ENELLKFSYI RTSFDKILLR WEPYWPPDFR DLLGFMLFYK EAPYQNVTEF DGQDACGSNS WTVVDIDPPL RSNDPKSQNH PGWLMRGLKP WTQYAIFVKT LVTFSDERRT YGAKSDIIYV QTDATNPSVP LDPISVSNSS SQIILKWKPP SDPNGNITHY LVFWERQAED SELFELDYCL KGLKLPSRTW SPPFESEDSQ KHNQSEYEDS AGECCSCPKT DSQILKELEE SSFRKTFEDY LHNVVFVPRP SRKRRSLGDV GNVTVAVPTV AAFPNTSSTS VPTSPEEHRP FEKVVNKESL VISGLRHFTG YRIELQACNQ DTPEERCSVA AYVSARTMPE AKADDIVGPV THEIFENNVV HLMWQEPKEP NGLIVLYEVS YRRYGDEELH LCVSRKHFAL ERGCRLRGLS PGNYSVRIRA TSLAGNGSWT EPTYFYVTDY LDVPSNIAKK LHHHHHH.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Insulin Human, His
ProSpec-NOV Human
- Description
Catalogue number
CYT-805
Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Introduction
Nephroblastoma Overexpressed which is encoded by the NOV gene is a part of the CCN family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
Description
Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.
Solubility
It is recommended to reconstitute the lyophilized NOV in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized NOV although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NOV should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein . Please prevent freeze-thaw cycles.
Purity
Greater than 95.0% as determined by: Analysis by RP-HPLC. Analysis by -PAGE.
Amino acid sequence
MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M.
Biological Activity
Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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NOV Human, HEK
ProSpec-NOV Human, HEK
- Description
Catalogue number
CYT-1032
Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Introduction
Nephroblastoma Overexpressed which is encoded by the NOV gene is a part of the CCN family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
Description
NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa .
Source
HEK293 cells.
Physical Appearance
Filtered White lyophilized powder.
Formulation
NOV filtered and lyophilized from 0.5mg/ml in PBS and 5 % trehalose.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. NOV is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
Purity
Greater than 90.0% as determined by -PAGE.
Amino acid sequence
QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEV SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH H.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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NOV Human
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NOV Mouse
ProSpec-Periostin Human
- Description
Catalogue number
CYT-452
Synonyms
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
Introduction
Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1 and bone morphogenetic protein . OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart.
Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart.
Description
The OSF2 His-Tagged Fusion Protein Human is produced in E. coli, and its molecular weight is 75 kDa protein containing 648 amino acid residues of the human OSF-2 and 23 additional amino acid residues – HisTag, Xa – cleavage site.
Source
Escherichia Coli.
Physical Appearance
Filtered White lyophilized powder.
Formulation
Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Solubility
It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Amino acid sequence
MGHHHHHHHH HHSSGHIEGR HMRNNHYDKI LAHSRIRGRD QGPNVCALQQ ILGTKKKYFS TCKNWYKKSI CGQKTTVLYE CCPGYMRMEG MKGCPAVLPI DHVYGTLGIV GATTTQRYSD ASKLREEIEG KGSFTYFAPS NEAWDNLDSD IRRGLESNVN VELLNALHSH MINKRMLTKD LKNGMIIPSM YNNLGLFINH YPNGVVTVNC ARIIHGNQIA TNGVVHVIDR VLTQIGTSIQ DFIEAEDDLS SFRAAAITSD ILEALGRDGH FTLFAPTNEA FEKLPRGVLE RFMGDKVASEALMKYHILNT LQCSESIMGG AVFETLEGNT IEIGCDGDSI TVNGIKMVNK KDIVTNNGVI HLIDQVLIPD SAKQVIELAG KQQTTFTDLV AQLGLASALR PDGEYTLLAP VNNAFSDDTL SMVQRLLKLI LQNHILKVKV GLNELYNGQI LETIGGKQLR VFVYRTAVCI ENSCMEKGSK QGRNGAIHIF REIIKPAEKS LHEKLKQDKR FSTFLSLLEA ADLKELLTQP GDWTLFVPTN DAFKGMTSEE KEILIRDKNA LQNIILYHLT PGVFIGKGFE PGVTNILKTT QGSKIFLKEV NDTLLVNELK SKESDIMTTN GVIHVVDKLL YPADTPVGND QLLEILNKLI KYIQIKFVRG STFKEIPVTV Y.
Purity
Greater than 90% as determined by -PAGE.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Related Products
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Periostin Human, HEK
ProSpec-RBP1 Human
- Description
Catalogue number
CYT-122
Synonyms
Retinol binding protein 1 cellular, CRBP, CRBP1, CRABP-I, RBPC.
Introduction
RBP1 is a member of the calycin superfamily and fatty-acid binding protein family. RBP1 is the carrier protein which takes part in the transport of retinol from the liver storage site to peripheral tissue. Additionally, RBP1 performs as a bridging molecule to recruit histone deacetylases which is a forceful regulator of gene expression. RBP1 is found in almost all the tissues with higher expression in pancreas, adrenal gland and pituitary gland, fetal liver and adult ovary.
Description
RBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids and having a molecular mass of 24.7kDa.
RBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
RBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
RBP1 protein solution containing 20mM Tris-HCl buffer , 200mM NaCl, 2mM DTT and 20% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
For long term storage it is recommended to add a carrier protein .
Avoid multiple freeze-thaw cycles.
Purity
Greater than 90% as determined by -PAGE.
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MGSMDPPAGF VRAGNPAVAA PQSPLSPEGA HFRAAHHPRS TGSRCPGSLQ PSRPLVANWL QSLPEMPVDF TGYWKMLVNE NFEEYLRALD VNVALRKIAN LLKPDKEIVQ DGDHMIIRTL STFRNYIMDF QVGKEFEEDL TGIDDRKCMT TVSWDGDKLQ CVQKGEKEGR GWTQWIEGDE LHLEMRVEGV VCKQVFKKVQ
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
DusQ2 CPG 500
DusQ2 CPG 500,This support is intended for automated synthesis of oligonucleotides with 3’-terminal DusQ2 quencher. Pore size of 500 Å is recommended for the synthesis of oligonucleotides of up to 50 bases in length.
- Products
- DNA
- CPG solid supports
- DusQ2 CPG 500
DusQ2 CPG 500
标签：CPG (controlled pore glass) solid supports for oligonucleotide synthesis
| 货号 | 规格 | 价格 | 货期 |
|---|---|---|---|
| 12960 | 100 mg | – | 7 days |
| 32960 | 500 mg | 530.00$ | in stock |
| 42960 | 1 g | 990.00$ | in stock |
| 52960 | 5 g | please inquire | in stock |
This support is intended for automated synthesis of oligonucleotides with 3’-terminal DusQ2 quencher. Pore size of 500 Å is recommended for the synthesis of oligonucleotides of up to 50 bases in length.
DusQ2 is a fluorescence quencher with absorption within the range of 560 to 670 nm. It is ideal for effective FRET quenching of fluorophores with emission in this range. The quencher is also used in hybridization probes with static and combined quenching. Its quenching effectiveness does not depend very much on overlapping of fluorophore and quencher spectra, thus allowing for effective quenching of the broad spectrum of fluorophores, including those with emission in the red and far-red part of the spectrum. Thus, DusQ2 can be used with such fluorophores (including but not limited to) as Cyanine3, TAMRA, ROX, Cyanine3.5, Quasar® 570, Pulsar® 650, Cyanine5, Quasar 670, Cyanine5.5, and Quasar 705.
该支持旨在用于自动合成具有 3′-末端 DusQ2 淬灭剂的寡核苷酸。 推荐 500 Å 的孔径用于合成长度不超过 50 个碱基的寡核苷酸。
DusQ2 是一种荧光猝灭剂，吸收范围为 560 至 670 nm。 它非常适合在此范围内发射荧光团的有效 FRET 猝灭。 猝灭剂还用于具有静态和组合猝灭的杂交探针。 其猝灭效果不太依赖于荧光团和猝灭剂光谱的重叠，因此可以有效猝灭广谱荧光团，包括在光谱的红色和远红色部分发射的荧光团。 因此，DusQ2 可以与诸如 Cyanine3、TAMRA、ROX、Cyanine3.5、Quasar® 570、Pulsar® 650、Cyanine5、Quasar 670、Cyanine5.5 和 Quasar 705 的荧光团（包括但不限于）一起使用。
Usage 用法
Coupling: Standard conditions identical to normal nucleobases.
Deprotection: 2 hours at room temperature using concentrated ammonia or 10 min at 65 °C using AMA mixture, concentrated aqueous ammonia/40% methylamine (1:1). Deprotection conditions depend on oligonucleotide composition and nucleobase protecting groups, as well as additional modifications, if present.
偶联：与正常核碱基相同的标准条件。
脱保护：在室温下使用浓氨水 2 小时或在 65°C 下使用 AMA 混合物、浓氨水/40% 甲胺 (1:1) 脱保护 10 分钟。 脱保护条件取决于寡核苷酸组成和核碱基保护基团，以及其他修饰（如果存在）。
Absorption spectrum of DusQ2
DusQ2 CPG 500相关产品
TFA-Amino modifier CPG 500
TFA-amino modifier CPG for oligo synthesis. 500 Å, high load controlled pore glass.
用于寡核苷酸合成的 TFA-氨基改性剂 CPG。 500 Å，高负载可控孔玻璃。
DusQ2 CPG 1000
Controlled pore glass (CPG) 1000 modified support for the synthesis of oligonucleotides with DusQ2 quencher at the 3’ end. Compatible with standard deblocking conditions.
可控孔玻璃 (CPG) 1000 改良后的 3′ 末端带有 DusQ2 淬灭剂的寡核苷酸合成支持。 与标准解块条件兼容。
FAM Phosphoramidite, 6-Isomer
Single isomer 6-FAM phosphoramidite for the synthesis of modified oligonucleotides.
用于合成修饰寡核苷酸的单一异构体 6-FAM 亚磷酰胺。
General properties
| Appearance: | dark blue beads |
| Quality control: | NMR 1H and HPLC-MS (95%) of bound reagent, loading measurement, functional testing in oligo synthesis. |
| Storage conditions: | Storage: 24 months after receival at -20°C in the dark. Transportation: at room temperature for up to 3 weeks. Avoid prolonged exposure to light. Desiccate.
储存：收到后 24 个月，在 -20°C 避光保存。 运输：在室温下长达 3 周。 避免长时间暴露在光线下。 干燥。 |
| MSDS: | Download |
| Product specifications |
Spectral properties
| Excitation/absorption maximum, nm: | 552 |
| ε, L⋅mol−1⋅cm−1: | 34000 |
| CF260: | 0.31 |
| CF280: | 0.26 |
Oligo synthesis details
| Pore size, Å: | 500 |
| Typical loading, umol/g: | 70−80 |