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SAE0046

Carboxypeptidase A

Cleaves C-terminal amino acids, suitable for Mass Spectrometry, from bovine pancreas

Synonym(s):

Carboxypeptidase A, Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase

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Size/SKUAvailabilityPrice
500 units
Please contact Customer Service for Availability
1 190,00 CZK
2500 units
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3 390,00 CZK
5000 units
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5 940,00 CZK

About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
MDL number:
Specific activity:
≥20 units/mg protein
Biological source:
bovine pancreas

1 190,00 CZK


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Product Name

Carboxypeptidase A from bovine pancreas, (Type II-PMSF treated), ≥20 units/mg protein

biological source

bovine pancreas

Quality Segment

form

aqueous suspension

quality

(Type II-PMSF treated)

specific activity

≥20 units/mg protein

mol wt

~35 kDa

purified by

2× crystallization

technique(s)

protein mass spectrometry: suitable

impurities

≤0.05 BTEE units/mg protein chymotrpsin, ≤10 BAEE units/mg protein trypsin

storage temp.

2-8°C

General description

Carboxypeptidase A (CPA) is a secreted protease is liberated after the activation of mast cells to facilitate acute anaphylaxis. Carboxypeptidase A has a long half-life in vivo, when compared to other secreted proteases.

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.
Carboxypeptidase A from bovine pancreas has been used in in vitro simulated digestion.

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 β-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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This Item
C9268C1261C5233
description

(Type II-PMSF treated), ≥20 units/mg protein

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

50-55 units/mg protein carboxypeptidase B

specific activity

≥20 units/mg protein

specific activity

≥50 units/mg protein

specific activity

≥6 units/mL packed gel, 25 °C

specific activity

50-55 units/mg protein carboxypeptidase B

biological source

bovine pancreas

biological source

-

biological source

enzyme from bovine pancreas

biological source

human pancreas

form

aqueous suspension

form

ready-to-use solution

form

ammonium sulfate suspension

form

solution

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

mol wt

~35 kDa

mol wt

~35 kDa

mol wt

~35,250

mol wt

-

purified by

2× crystallization

purified by

2× crystallization

purified by

-

purified by

-


Pictograms

Health hazard

Signal Word

Danger

Hazard Codes

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

WGK

WGK 2

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

108-88-3

CAS No.


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