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C9584

Sigma-Aldrich

Carboxypeptidase B from porcine pancreas

lyophilized powder

Synonym(s):

Peptidyl-L-lysine(L-arginine) hydrolase, Protaminase

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About This Item

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

biological source

Porcine pancreas

Quality Level

grade

Proteomics Grade

form

lyophilized powder

specific activity

≥125 units/mg protein

mol wt

34,000 Da± 600

purified by

affinity chromatography

composition

Protein, 40-70%

foreign activity

carboxypeptidase A ≤1%
chymotrypsin ≤0.1%
trypsin ≤5%

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

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Application

Carboxypeptidase B has been used in a study to develop a non-invasive pregnancy assay for use in both captive and wild polar bears. Carboxypeptidase B has been used in a study that identified new potential biomarkers of acute pancreatitis.
The enzyme from Sigma has been used to develop homogeneous time-resolved fluorescence (HTRF) assay for measuring carboxypeptidase B activity in a miniaturized high-throughput screening format. It has been used to evaluate the impact of the C-terminal lysine(s) in human plasminogen binding to Bifidobacterium. The effect of treatment with carboxypeptidase B, which is a C-terminal lysine-specific endopeptidase, is measured using flow cytometry analysis.

Biochem/physiol Actions

Carboxypeptidase B is a proteolytic enzyme capable of rapidly hydrolyzing peptide bonds to release certain carboxyl-terminal basic amino acids from peptides and proteins. Its molecular mass is 34,300±600 Da. It contains one non-dialyzable gram atom of zinc per mole. The enzyme activity is inhibited by metal chelating agents 1, 10-phenanthroline, 8-hydroxyquinoline-5-sulfonic acid, and 2,2′-dipyridyl.

Packaging

Package size based on protein content

Unit Definition

One unit will hydrolyze 1.0 μmole of hippuryl-L-arginine per min at pH 7.65 at 25 °C.

Physical form

Contains HEPES buffer salts, zinc chloride and carbohydrate

Preparation Note

Treated with protease inhibitor, AEBSF, to eliminate serine protease activity.

Analysis Note

Protein determined by biuret.

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves


Certificates of Analysis (COA)

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Marc Ferrer et al.
Analytical biochemistry, 317(1), 94-98 (2003-05-06)
An epitope-unmasking, homogeneous time-resolved fluorescence (HTRF) assay has been developed for measuring carboxypeptidase B (CPB) activity in a miniaturized high-throughput screening format. The enzyme substrate (biotin-RYRGLMVGGVVR-OH) is cleaved by CPB at the C terminus, causing release of the C-terminal Arg
Andrew Lee et al.
Langmuir : the ACS journal of surfaces and colloids, 27(18), 11560-11574 (2011-08-13)
This article describes the use of capillary electrophoresis (CE) to examine the influence of different cations (C(+); C(+) = Na(+) and tetra-n-alkylammonium, NR(4)(+), where R = Me, Et, Pr, and Bu) on the rates of denaturation of bovine carbonic anhydrase
E Curry et al.
Theriogenology, 78(2), 308-314 (2012-04-28)
Currently, there is no method of accurately and non-invasively diagnosing pregnancy in polar bears. Specific proteins may exhibit altered profiles in the feces of pregnant bears, but predicting appropriate candidate proteins to investigate is speculative at best. The objective of
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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