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C5233

Sigma-Aldrich

Carboxypeptidase B from human pancreas

50-55 units/mg protein carboxypeptidase B

Synonym(s):

Peptidyl-L-Lysine[L-arginine] hydrolase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.54

biological source

human pancreas

Quality Level

form

solution

specific activity

50-55 units/mg protein carboxypeptidase B

impurities

≤0.2% chymotrypsin
≤0.2% trypsin
≤1 unit/mg protein carboxypeptidase A

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

InChI

1S/C31H38N4O7S/c1-20(32-26(36)15-16-27(37)38)28(39)33-21(2)30(41)35-17-9-14-25(35)29(40)34-24(18-22-10-5-3-6-11-22)31(42)43-19-23-12-7-4-8-13-23/h3-8,10-13,20-21,24-25H,9,14-19H2,1-2H3,(H,32,36)(H,33,39)(H,34,40)(H,37,38)

InChI key

TWURVFFNODFJBJ-UHFFFAOYSA-N

Gene Information

human ... CPB1(1360)

General description

Carboxypeptidase B is mapped to human chromosome 3q24. Carboxypeptidase B belongs to A/B subfamily of carboxypeptidases.

Application

Carboxypeptidase B from Sigma has been used as a reference for assaying carboxypeptidase activity in lysed pituitary granules derived from the anterior and intermediate lobes of rat. The enzyme has also been used to digest plasma samples by removing C-terminal basic amino acids, to get a distinct band for each allotype during C4 electrophoresis.

Biochem/physiol Actions

Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34,000 Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis.
Mutations in the carboxypeptidase B (CPB1) gene is implicated with increased susceptibility to pancreatic cancer development and progression. Elevated levels of CPB1 is associated with low grade breast tumors and lymph node positive grade 1 tumors.

Unit Definition

One unit will hydrolyze 1 μmole of hippuryl-L-arginine per minute at pH 7.7 at 25 °C

Physical form

Solution in 0.05 M NaOAc pH 5.0 + 1.0 M NaCl + 0.01% NaN3

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Human procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI)
Pereira PJB, et al.
Journal of Molecular Biology, 321(3), 537-547 (2002)
Combined proteomics and transcriptomics identifies carboxypeptidase b1 and nuclear factor kappaB (NF-kappaB) associated proteins as putative biomarkers of metastasis in low grade breast cancer
Bouchal P, et al.
Molecular and Cellular Proteomics, 14(7), 1814-1830 (2015)
Claes Hjalmarsson et al.
Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.], 9(5), 700-707 (2009-08-18)
The concentration of carboxypeptidase B activation peptide (CAPAP) is proposed to be a predictor of severe acute pancreatitis. The activated protein C (APC)-protein C inhibitor (PCI; APC-PCI) complex in plasma could be useful in detecting the hypercoagulative condition in severe
Anna Rozhkova
Journal of chromatography. A, 1216(32), 5989-5994 (2009-06-30)
A robust cation-exchange chromatofocusing method was developed for the routine analysis of a recombinant humanized monoclonal IgG antibody. We compare the chromatofocusing method to the conventional cation-exchange chromatography (CEX) employing a salt gradient and show clear advantages of chromatofocusing over
Mutations in the pancreatic secretory enzymes CPA1 and CPB1 are associated with pancreatic cancer
Tamura K, et al.
Proceedings of the National Academy of Sciences of the USA, 201720588-201720588 (2018)

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