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Key Documents

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Safety Information

C9268

Sigma-Aldrich

Carboxypeptidase A from bovine pancreas

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

Synonym(s):

Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase

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10 G
¥626.68
25 G
¥634.47
100 G
¥3,511.98

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Estimated to ship on2025年4月27日Details

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10 G
¥626.68
25 G
¥634.47
100 G
¥3,511.98

About This Item

CAS Number:
11075-17-5
Enzyme Commission number:
3.4.17.1 (BRENDA, IUBMB)
MDL number:
MFCD00130718
UNSPSC Code:
12352204
NACRES:
NA.54

¥626.68

Estimated to ship on2025年4月27日Details

Request a Bulk Order

grade

Proteomics Grade

Quality Level

300

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

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1 of 4

This Item
N4876NX0403106762
Ninhydrin ACS reagent

151173

Ninhydrin

Ninhydrin suitable for amino acid detection

N4876

Ninhydrin

Ninhydrin

NX0403

Ninhydrin

Ninhydrin GR for analysis ACS,Reag. Ph Eur

106762

Ninhydrin

Quality Level

200

Quality Level

200

Quality Level

100

Quality Level

100

solubility

H2O: passes test

solubility

ethanol: 100 mg/mL, H2O: 50 mg/mL (with sonication)

solubility

-

solubility

-

form

solid

form

powder

form

-

form

solid

mp

250 °C (dec.) (lit.)

mp

250 °C (dec.) (lit.)

mp

-

mp

250-258 °C (decomposition)

grade

ACS reagent

grade

-

grade

-

grade

ACS reagent

description

identification and melting point passes test

description

-

description

-

description

-

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]

Unit Definition

One unit will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 at 25 °C.

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

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

动植物源性产品
  • Specification Sheet

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    Certificates of Analysis (COA)

    Lot/Batch Number
    0000292966
    SLCD2357
    0000292966
    0000292968
    0000292969

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    Bodo Wiesler et al.
    The Plant journal : for cell and molecular biology, 32(6), 1023-1032 (2002-12-21)
    Auxin controls the orientation of cortical microtubules in maize coleoptile segments. We used tyrosinylated alpha-tubulin as a marker to assess auxin-dependent changes in microtubule turnover. Auxin-induced tyrosinylated alpha-tubulin, correlated with an elevated sensitivity of growth to antimicrotubular compounds such as
    Brian P Austin et al.
    Protein expression and purification, 77(1), 53-61 (2010-11-16)
    Carboxypeptidases may serve as tools for removal of C-terminal affinity tags. In the present study, we describe the expression and purification of an A-type carboxypeptidase from the fungal pathogen Metarhizium anisopliae (MeCPA) that has been genetically engineered to facilitate the
    Laurence Lafanechère et al.
    Methods in molecular biology (Clifton, N.J.), 777, 71-86 (2011-07-21)
    Alpha tubulin comprises a C-terminal tyrosine residue, which is subject to cyclic removal from the peptide chain by a still uncharacterized carboxypeptidase and re-addition to the chain by a tubulin tyrosine ligase. We have shown in different animal or human
    Matthew A Cottee et al.
    Nature communications, 12(1), 5590-5590 (2021-09-24)
    Excessive replication of Saccharomyces cerevisiae Ty1 retrotransposons is regulated by Copy Number Control, a process requiring the p22/p18 protein produced from a sub-genomic transcript initiated within Ty1 GAG. In retrotransposition, Gag performs the capsid functions required for replication and re-integration.
    Kaia Kukk et al.
    Journal of biotechnology, 231, 224-231 (2016-06-19)
    Vertebrate prostaglandin H synthases (PGHSs) are membrane-bound disulphide-containing hemoglycoproteins. Therefore, eukaryotic expression systems are required for the production of recombinant PGHSs. Recently we announced the expression of human PGHS-2 (hPGHS-2) in the yeast Pichia pastoris. Here we report improved production
    View All Related Papers

    Protocols

    Enzymatic Assay: Carboxypeptidase

    Carboxypeptidase A activity measured via continuous spectrophotometric rate determination assay with hippuryl-L-phenylalanine substrate.

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