Please see the links below for the Product Information Sheet which is located in the 'DOCUMENTATION' section under 'More Documents':
https://www.sigmaaldrich.com/product/sigma/c9268#product-documentation
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/422/794/c9268enz.pdf
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C9268
Carboxypeptidase A aus Rinderpankreas
(Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution
Synonym(e):
Carboxypolypeptidase, Peptidyl-L-aminosäure-Hydrolase
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| Ihnen/SKU | Verfügbarkeit | Preis |
|---|---|---|
500 units | Warenkorb auf Verfügbarkeit prüfen | CHF 145.00 |
2500 units | Warenkorb auf Verfügbarkeit prüfen | CHF 272.00 |
5000 units | Warenkorb auf Verfügbarkeit prüfen | CHF 549.00 |
Über diesen Artikel
CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥50 units/mg protein
Technischer Dienst
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Unterstützung erhaltengrade
Proteomics Grade
form
ready-to-use solution
quality
(Type II-PMSF treated)
specific activity
≥50 units/mg protein
mol wt
~35 kDa
purified by
2× crystallization
impurities
≤0.05 BTEE units/mg protein chymotrypsin, ≤10 BAEE units/mg protein trypsin
storage temp.
2-8°C
Application
Carboxypeptidase A from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase A in Escherichia coli. Carboxypeptidase A from bovine pancreas has also been used in a study to investigate the isolation and partial characterization of precursor forms of ostrich carboxypeptidase.
The enzyme from Sigma has been used as a comparison to study the specificity of Metarhizium anisopliae carboxypeptidase A (MeCPA). MeCPA had been genetically engineered to facilitate the removal of polyhistidine tags from the C-termini of recombinant proteins.[1] It has also been used to de-tyrosinate α-tubulin, in vitro, in order to induce high affinity to ethyl-N-phenylcarbamate (EPC) sepharose.[2]
Biochem/physiol Actions
Carboxypeptidase as isolated from bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by beta-phenylpropionate and indole acetate.[3]
Preparation Note
Treated with phenylmethylsulfonyl fluoride to eliminate trypsin and chymotrypsin activity. Dialyzed and recrystallized: aqueous suspension with toluene added.
Analysis Note
Protein determined by E1%/278
Other Notes
One unit will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 at 25 °C.
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Dieser Artikel | |||
|---|---|---|---|
| specific activity ≥50 units/mg protein | specific activity ≥125 units/mg protein | specific activity ≥6 units/mL packed gel, 25 °C | specific activity ≥10,000 BAEE units/mg protein |
| grade Proteomics Grade | grade Proteomics Grade | grade - | grade Proteomics Grade |
| form ready-to-use solution | form lyophilized powder | form ammonium sulfate suspension | form essentially salt-free, lyophilized powder |
| mol wt ~35 kDa | mol wt 34,000 Da± 600 | mol wt ~35,250 | mol wt 23.8 kDa |
| storage temp. 2-8°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C |
| impurities ≤0.05 BTEE units/mg protein chymotrypsin, ≤10 BAEE units/mg protein trypsin | impurities - | impurities - | impurities - |
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