| Description | Biochemical Test:SDS-PAGE (purity> 85%); Western blot with i: anti-Ku autoantibody positive sample; ii: monoclonal anti His-tag antibody.Calculated Isoelectric Point:p70 subunit: pH 6.3; p80 subunit: pH 5.7; p70/p80 heterodimer: around pH 6.0Coating Concentration:0.2-0.6 µg/ml (depending on Biochemical Test:SDS-PAGE (purity> 85%); Western blot with i: anti-Ku autoantibody positive sample; ii: monoclonal anti His-tag antibody.Calculated Isoelectric Point:p70 subunit: pH 6.3; p80 subunit: pH 5.7; p70/p80 heterodimer: around pH 6.0Coating Concentration:0.2-0.6 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups... Read More | Inquire | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.ApplicationUseful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.Reported useful for the isolation of hepatic, yeast, and mung bean mitochondriaDetermination of enzyme localization on membranesTreatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research... Read More | Purity>95% as determined by SDS-PAGE and Coomassie blue stainingFunctionThe heparin-binding fibroblast growth factors play important roles in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. They are potent mitogens in vitro.Sequence Purity>95% as determined by SDS-PAGE and Coomassie blue stainingFunctionThe heparin-binding fibroblast growth factors play important roles in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. They are potent mitogens in vitro.Sequence similaritiesBelongs to the heparin-binding growth factors family.Cellular localizationSecreted. Cytoplasm. Cytoplasm > cell cortex. Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1... 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 |