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C9584 Sigma

Carboxypeptidase B from porcine pancreas

lyophilized powder

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

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Enzyme Class Index,
InChI Key   TWURVFFNODFJBJ-UHFFFAOYSA-N
form   lyophilized powder
activity   ≥125 units/mg protein
purified by   affinity chromatography
composition   Protein, 40-70%
foreign activity   carboxypeptidase A ≤1%
  chymotrypsin ≤0.1%
  trypsin ≤5%
storage temp.   −20°C

Description

Frequently Asked Questions

Frequently Asked Questions are available for this Product.

Analysis Note

Protein determined by biuret.

Packaging

1, 5 mg in glass bottle

Package size based on protein content

Preparation Note

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

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

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.

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Biomedical Applications
Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
3

Frequently Asked Questions

Which document(s) contains shelf-life or expiration date information for a given product?
If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis. These documents are located on the product detail page under Useful Links & Tools. Click on the following link to search for a Certificate of Analysis. Please click the following link to see the details on our Product Dating Information.
How do I get lot-specific information or a Certificate of Analysis?
A Certificate of Analysis is available by lot number and can be obtained through our Advanced Search Option: http://www.sigmaaldrich.com/catalog/AdvancedSearchPage.do
How do I find price and availability?
There are several ways to find pricing and availability for our products.  Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers. 
What is the Department of Transportation shipping information for this product?
Transportation information can be found in Section 14 of the product's (M)SDS. To access the shipping information for this material, use the link on the product detail page for the product, or search here. 
My question is not addressed here, how can I contact Technical Service for assistance?
Use the option to the right to "Ask a Question" by email of a Technical Service Scientist.
Can Product C9584, Carboxypeptidase B from porcine pancreas be used to remove basic C-terminal residues of tryptic peptides?
The use of Product C9584, Carboxypeptidase B from porcine pancreas to remove basic C-terminal residues of tryptic peptides has been described in the literature.  Please see the following as an example: The Protein Protocols Handbook, J.M. Walker, Ed., pp. 569, Humana Press, Totawa NJ (1996)
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Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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