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Merck

C9268

Carboxypeptidase A from bovine pancreas

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

Sinónimos:

Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase

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500 UNITS

US$ 189,00

2500 UNITS

US$ 378,00

5000 UNITS

US$ 696,00

US$ 189,00

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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
Número CE:
MDL number:
Specific activity:
≥50 units/mg protein

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grade

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

Quality Level

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1 of 4

Este artículo
C9584C1261T1426
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

Quality Level

300

Quality Level

200

Quality Level

200

Quality Level

300

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.

used together

Referencia del producto
Descripción
Precios

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Clase de almacenamiento

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter


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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
Facile discovery of surrogate cytokine agonists.
Yen, et al.
Cell, 185, 1414-1430 (2023)
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.

Protocolos

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

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Questions

  1. In which solution and at what concentration should this product be reconstituted? How long is the stock solution stable and how should it be stored?

    1 answer
    1. 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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