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Merck

C5233

Sigma-Aldrich

Carboxypeptidase B from human pancreas

50-55 units/mg protein carboxypeptidase B

Sinónimos:

Peptidyl-L-Lysine[L-arginine] hydrolase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
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

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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'
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)
Lawrence L K Leung et al.
Advances in experimental medicine and biology, 632, 61-69 (2008-11-26)
Thrombin-activatable procarboxypeptidase B (proCPB or thrombin-activatable fibrinolysis inhibitor or TAFI) is a plasma procarboxypeptidase that is activated by the thrombin-thrombomodulin complex on the vascular endothelial surface. The activated CPB removes the newly exposed carboxyl terminal lysines in the partially digested
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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