Carboxypeptidase B from Porcine Pancreas

<strong>Carboxypeptidase B from Porcine Pancreas</strong>_x000D_ <strong>Catalog number:</strong> B2014087_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 1 mg_x000D_ <strong>Molecular Weight or Concentration:</strong> 170 U/mg_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20°C_x000D_ <strong>Keywords:</strong> Carboxypeptidase B_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Z_hlke H, Steiner DF, Lernmark A, Lipsey C. Carboxypeptidase B-like and trypsin-like activities in isolated rat pancreatic islets Ciba Found Symp. 1976;41:183-95._x000D_ 2: Chen L, Shan Y, Yang C, Sui Z, Zhang X, Zhang L, Zhang Y. Carboxypeptidase B-Assisted Charge-Based Fractional Diagonal Chromatography for Deep Screening of C-Terminome Anal Chem. 2020 Jun 16;92(12):8005-8009._x000D_ 3: Deng L, Wang L, Yong F, Xiong J, Jin T, De La Iglesia-Garcia D, Bharucha S, Altaf K, Huang W, Xia Q. Prediction of the severity of acute pancreatitis on admission by carboxypeptidase-B activation peptide: A systematic review and meta-analysis Clin Biochem. 2015 Jul;48(10-11):740-6._x000D_ 4: Zhang Y, Han K, Du C, Li R, Liu J, Zeng H, Zhu L, Li A. Carboxypeptidase B blocks ex vivo activation of the anaphylatoxin-neutrophil extracellular trap axis in neutrophils from COVID-19 patients Crit Care. 2021 Feb 8;25(1):51._x000D_ 5: Leung LL, Myles T, Nishimura T, Song JJ, Robinson WH. Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI) Mol Immunol. 2008 Oct;45(16):4080-3._x000D_ 6: Zhang X, Zhang L, Li J. Peptide-modified nanochannel system for carboxypeptidase B activity detection Anal Chim Acta. 2019 May 30;1057:36-43._x000D_ 7: Hook VY, Loh YP. Carboxypeptidase B-like converting enzyme activity in secretory granules of rat pituitary Proc Natl Acad Sci U S A. 1984 May;81(9):2776-80._x000D_ 8: Akparov V, Sokolenko N, Timofeev V, Kuranova I. Structure of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine Acta Crystallogr F Struct Biol Commun. 2015 Oct;71(Pt 10):1335-40._x000D_ 9: Muto Y, Suzuki K, Sato E, Ishii H. Carboxypeptidase B inhibitors reduce tissue factor-induced renal microthrombi in rats Eur J Pharmacol. 2003 Feb 14;461(2-3):181-9._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/16960106">10: Mosnier LO, Bouma BN. Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis Arterioscler Thromb Vasc Biol. 2006 Nov;26(11):2445-53. </a>_x000D_ _x000D_ <strong>Products Related to Carboxypeptidase B from Porcine Pancreas can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>