||Full length native protein , corresponding to amino acids 23-423 of Human Carboxypeptidase B2.
||Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. Available sequence data analyses indicate splice variants that encode different isoforms.
||400 amino acids
||Specific Activity: 2.0-9.2 units/mg. Specific activity is determined by a kinetic assay using Hippuryl-L-Arginine as substrate.One unit equals one micromole of Hippuryl-L-Arginine hyrolyzed per minute.Specific activity is reported in Units per milligram.
||>95% by SDS-PAGE
||Preservative: NoneConstituents: 20mM HEPES, 150mM Sodium chloride, pH 7.4
||Shipped on dry ice. Upon delivery aliquot and store at -80oC. Avoid freeze / thaw cycles.