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C9268
Carboxypeptidase A from bovine pancreas
(Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution
Synonyme(s) :
Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase
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| Taille/Référence | Disponibilité | Prix |
|---|---|---|
500 units | Veuillez contacter notre Service Clients pour connaître la disponibilité de ce produit. | 119,00 € |
2500 units | Veuillez contacter notre Service Clients pour connaître la disponibilité de ce produit. | 401,00 € |
5000 units | Veuillez contacter notre Service Clients pour connaître la disponibilité de ce produit. | 435,00 € |
A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥50 units/mg protein
119,00 €
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Proteomics Grade
Quality Segment
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
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. It has also been used to de-tyrosinate α-tubulin, in vitro, in order to induce high affinity to ethyl-N-phenylcarbamate (EPC) sepharose.
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.
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.
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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Cet article | |||
|---|---|---|---|
| description (Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution | description ammonium sulfate suspension, ≥6 units/mL packed gel, 25 °C, enzyme from bovine pancreas | description TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein | description (Type II-PMSF treated), ≥20 units/mg protein |
| specific activity ≥50 units/mg protein | specific activity ≥6 units/mL packed gel, 25 °C | specific activity ≥10,000 BAEE units/mg protein | specific activity ≥20 units/mg protein |
| grade Proteomics Grade | grade - | grade Proteomics Grade | grade - |
| form ready-to-use solution | form ammonium sulfate suspension | form essentially salt-free, lyophilized powder | form aqueous suspension |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. −20°C | storage temp. 2-8°C |
| mol wt ~35 kDa | mol wt ~35,250 | mol wt 23.8 kDa | mol wt ~35 kDa |
| impurities ≤10 BAEE units/mg protein trypsin, ≤0.05 BTEE units/mg protein chymotrypsin | impurities - | impurities - | impurities ≤10 BAEE units/mg protein trypsin, ≤0.05 BTEE units/mg protein chymotrpsin |
Listes réglementaires
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108-88-3
CAS No.
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