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Key Documents

C5233

Sigma-Aldrich

Carboxypeptidase B from human pancreas

50-55 units/mg protein carboxypeptidase B

Sinonimo/i:

Peptidyl-L-Lysine[L-arginine] hydrolase

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero MDL:
Codice UNSPSC:
12352204
ID PubChem:
NACRES:
NA.54

Origine biologica

human pancreas

Livello qualitativo

Forma fisica

solution

Attività specifica

50-55 units/mg protein carboxypeptidase B

Impurezze

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

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−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)
TWURVFFNODFJBJ-UHFFFAOYSA-N

Informazioni sul gene

human ... CPB1(1360)

Descrizione generale

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

Applicazioni

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.

Azioni biochim/fisiol

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.

Definizione di unità

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

Stato fisico

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

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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
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Molecular and Cellular Proteomics, 14(7), 1814-1830 (2015)
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)
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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'
Mutations in the pancreatic secretory enzymes CPA1 and CPB1 are associated with pancreatic cancer
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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

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