Skip to Content
MilliporeSigma

Key Documents

View All Documentation

Skip To

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

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View
Size/SKUAvailabilityPrice
500 units

Available to ship TODAYfromMILWAUKEE

$51.70
2500 units

Available to ship TODAYfromMILWAUKEE

$154.00
5000 units

Available to ship TODAYfromMILWAUKEE

$259.00

About This Item

CAS Number:
11075-17-5
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
3.4.17.1 (BRENDA, IUBMB)
MDL number:
MFCD00130718
Specific activity:
≥20 units/mg protein
Biological source:
bovine pancreas

$51.70

Available to ship TODAYDetails

​
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

Product Name

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

biological source

bovine pancreas

Quality Segment

200

form

aqueous suspension

quality

(Type II-PMSF treated)

specific activity

≥20 units/mg protein

mol wt

~35 kDa

purified by

2× crystallization

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.

Compare Similar Items

View Full Comparison

Show Differences

1 of 1

This Item
C9584C9268CHY5S
Carboxypeptidase A from bovine pancreas (Type II-PMSF treated), ≥20 units/mg protein

Sigma-Aldrich

SAE0046

Carboxypeptidase A from bovine pancreas

Carboxypeptidase B from porcine pancreas lyophilized powder

Sigma-Aldrich

C9584

Carboxypeptidase B from porcine pancreas

Carboxypeptidase A from bovine pancreas (Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution

Sigma-Aldrich

C9268

Carboxypeptidase A from bovine pancreas

α-Chymotrypsin from bovine pancreas ≥40 units/mg protein, vial of 5 mg

Sigma-Aldrich

CHY5S

α-Chymotrypsin from bovine pancreas

description

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

description

lyophilized powder

description

(Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution

description

≥40 units/mg protein, vial of 5 mg

biological source

bovine pancreas

biological source

Porcine pancreas

biological source

-

biological source

bovine pancreas

specific activity

≥20 units/mg protein

specific activity

≥125 units/mg protein

specific activity

≥50 units/mg protein

specific activity

≥40 units/mg protein

form

aqueous suspension

form

lyophilized powder

form

ready-to-use solution

form

solid

mol wt

~35 kDa

mol wt

34,000 Da± 600

mol wt

~35 kDa

mol wt

25 kDa

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

impurities

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

impurities

-

impurities

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

impurities

-

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

It looks like we've run into a problem, but you can still download Certificates of Analysis from our Documents section.

If you need assistance, please contact Customer Support

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Questions

Reviews

No rating value

Active Filters