| Description | FCGBP Human Pre-designed siRNA Set A contains three designed siRNAs for FCGBP gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components FCGBP siRNA-1: 5 nmol (HPLC) FCGBP siRNA-2: 5 nmol (HPLC) FCGBP siRNA-3: 5 nmol (HPLC) siRNA Negative Control:FCGBP Human Pre-designed siRNA Set A contains three designed siRNAs for FCGBP gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components FCGBP siRNA-1: 5 nmol (HPLC) FCGBP siRNA-2: 5 nmol (HPLC) FCGBP siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is also inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B (EC 3.4.17.2) is expressed in E.Coli and purified by high pressure liquid chromatography. There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. No protease inhibitors such as PMSF are present in the preparation.Animal origin free:eliminate the risk of virus presence, or of any other potential adventitious agents found in animal-derived carboxypeptitase B.Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. High purity:1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating protease activities found in extracted enzymes with lower purity level. 2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A. 3）Less than 10ppm of recombinant trypsin... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Human B7 homolog 3 (B7-H3) is a member of the B7 family of immune proteins that provide signals for the regulation of immune responses. Other family members include B7-1, B7-2, B7-H1/PD-L1, B7-H2, and PD-L2. B7 Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Human B7 homolog 3 (B7-H3) is a member of the B7 family of immune proteins that provide signals for the regulation of immune responses. Other family members include B7-1, B7-2, B7-H1/PD-L1, B7-H2, and PD-L2. B7 family proteins are type I transmembrane immunoglobulin (Ig) superfamily members that contain extracellular Ig V‑like and Ig C‑like domains with a short cytoplasmic tail. Among the family members there is about 20 - 40% amino acid (aa) sequence identity. B7-H3 was initially reported to be a 316 aa type I transmembrane precursor protein that contained a signal sequence, an extracellular region with one V‑type and one C‑type Ig domain, a transmembrane segment and a short cytoplasmic tail. Subsequent studies have identified a second 110 kDa form whose precursor is 534 aa in length. Termed 4IgB7-H3 or B7-H3b, this molecule has two additional Ig-like domains (one V‑type and one C‑type) and shows a ubiquituous expression pattern. It would appear that the human 4Ig form is the principal, if not the only form of B7-H3. Its precursor contains a 26 aa signal sequence, a 435 aa extracellular region, a 31 aa transmembrane domain, and a 42 aa cytoplasmic tail. The four Ig-like domains alternate between V‑type and C‑type, and apparently are the consequence of a V‑C type tandem duplication. B7-H3b is expressed on dendritic cells as well as activated T, B and NK cells. The mouse gene differs from that of human in that it cannot code for four Ig-like domains; only a V‑type:C‑type pair. Human B7-H3b binding to an undefined receptor has shown to be inhibitory to NK cell illing and cytokine release. It also seems to be required for late stage osteoblast differentiation... Read More | Purity> 95 % by SDS-PAGE and HPLC analyses.FunctionPromotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix Purity> 95 % by SDS-PAGE and HPLC analyses.FunctionPromotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5. CYR61-mediated gene regulation is dependent on heparin-binding. Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1. Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-v/beta-5 and cell proliferation through integrin alpha-v/beta-3.Banckground:Cyr61, also known as CCN1, is a 40-45 kDa matricellular glycoprotein that plays an important role in cellular adhesion and migration (1). Cyr61 consists of an IGFBP domain, a VWF type C domain, a TSP type I domain, and a cysteine knot domain (2). Mature human Cyr61 shares 93% amino acid sequence identity with mouse and rat Cyr61. It is widely expressed during development and in adult tissues (2, 3). Cyr61 associates with the extracellular matrix (ECM) and with many cell surface molecules including Integrins alpha V beta 3, alpha V beta 5, alpha M beta 2, and alpha 6 beta 1, Syndecan-4, and heparan sulfate proteoglycans (1, 3). Cyr61 mediates the adhesion and migration of multiple cell types and also promotes vascular endothelial cell tubule formation (4-6). Plasmin cleavage of ECM-bound Cyr61 releases a 28 kDa N-terminal fragment which retains the ability to promote endothelial cell migration (7). Cyr61 exhibits both tumorigenic and tumor suppressor properties. It is up-regulated and promotes tumorigenesis, angiogenesis, and metastasis in breast, renal, gastric, squamous cell, and colorectal carcinomas as well as in glioma (8-12). In contrast, whendown-regulated, it suppresses tumor growth in endometrial, hepatic, and non-small cell lung cancers (8, 13, 14). Cyr61 is also up-regulated in injured skin and bone where it induces the expression of growth factors, cytokines, proteases, and integrins involved in wound repair (15, 16)... Read More | Purity>95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose Purity>95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.Post-translationalHydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting. HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation... Read More |