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C5233

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:
9025-24-5
UNSPSC Code:
12352204
PubChem Substance ID:
24892769
NACRES:
NA.54
EC Number:
3.4.17.2 (BRENDA, IUBMB)
MDL number:
MFCD00081476
Specific activity:
50-55 units/mg protein carboxypeptidase B
Biological source:
human pancreas

Key Documents

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Product Name

Carboxypeptidase B from human pancreas, 50-55 units/mg protein carboxypeptidase B

SMILES string

S(Cc3ccccc3)C(=O)C(NC(=O)C2N(CCC2)C(=O)C(NC(=O)C(NC(=O)CCC(=O)O)C)C)Cc1ccccc1

InChI key

TWURVFFNODFJBJ-UHFFFAOYSA-N

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)

biological source

human pancreas

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.

P15086

shipped in

dry ice

storage temp.

−20°C

Quality Level

200

Gene Information

human ... CPB1(1360)

Related Categories

General description

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

Other Notes

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

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.

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
0000316875
0000307403
0000307403
0000316875
SLCJ4634

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E Sim et al.
The Biochemical journal, 239(3), 763-767 (1986-11-01)
The plasma complement protein C4 is encoded at two highly polymorphic loci, A and B, within the class-III region of the major histocompatibility complex. At least 34 different polymorphic variants of human C4 have been identified, including non-expressed or 'null'
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)
Xiu Qin Xu et al.
The Journal of biological chemistry, 280(25), 23987-24003 (2005-04-23)
We have exploited a discrepancy in the oncogenic potential of autocrine and exogenous human growth hormone (hGH) in an attempt to identify molecules that could potentially be involved in oncogenic transformation of the human mammary epithelial cell. Microarray analysis of
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)
Saurabh Chatterjee et al.
Free radical biology & medicine, 46(4), 454-461 (2008-12-04)
Post-translational modification of proteins due to exposure to radicals and other reactive species are markers of metabolic and inflammatory oxidative stress such as sepsis. This study uses the nitrone spin-trap DMPO and a combination of immuno-spin trapping and mass spectrometry
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