| Description | Biochemical Test:SDS-PAGE (purity > 80%); Western-Blot with patient sampleCalculated Isoelectric Point:pH 6.2 | Purity>95% SDS-PAGEFunctionLipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 kD subunit. This cytokine is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. IL12 has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Recombinant human IL12 protein, fused to His-tag at C-terminus, was expressed in insect cells using baculovirus expression system and purified by using conventional chromatography techniques... Read More | Purity>97% by SDS-PAGE and HPLC analyses.Additional sequence informationN-terminal Glycine.FunctionChemotactic for monocytes and T-lymphocytes. Binds to CXCR3.Post-translationalCXCL10(1-73) is produced by proteolytic cleavage after secretion from keratinocytes | Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |