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C9268

Sigma-Aldrich

Carboxypeptidase A from bovine pancreas

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

Sinonimo/i:

Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase

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About This Item

Numero CAS:
11075-17-5
Classificazione EC (Enzyme Commission):
3.4.17.1 (BRENDA, IUBMB)
Numero MDL:
MFCD00130718
Codice UNSPSC:
12352204
NACRES:
NA.54

Grado

Proteomics Grade

Forma fisica

ready-to-use solution

Qualità

(Type II-PMSF treated)

Attività specifica

≥50 units/mg protein

PM

~35 kDa

Purificato mediante

2× crystallization

Impurezze

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

Temperatura di conservazione

2-8°C

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Categorie correlate

Applicazioni

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. It has also been used to de-tyrosinate α-tubulin, in vitro, in order to induce high affinity to ethyl-N-phenylcarbamate (EPC) sepharose.

Azioni biochim/fisiol

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.

Definizione di unità

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

Nota sulla preparazione

Treated with phenylmethylsulfonyl fluoride to eliminate trypsin and chymotrypsin activity. Dialyzed and recrystallized: aqueous suspension with toluene added.

Risultati analitici

Protein determined by E1%/278

Inibitore

N° Catalogo
Descrizione
Determinazione del prezzo

Substrato

N° Catalogo
Descrizione
Determinazione del prezzo

H6875

Hippuryl-L-phenylalanine

Pittogrammi

Health hazard
GHS08

Avvertenze

Danger

Indicazioni di pericolo

H334

Classi di pericolo

Resp. Sens. 1

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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

Certificati d'analisi (COA)

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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
Heiko Witt et al.
Nature genetics, 45(10), 1216-1220 (2013-08-21)
Chronic pancreatitis is an inflammatory disorder of the pancreas. We analyzed CPA1, encoding carboxypeptidase A1, in subjects with nonalcoholic chronic pancreatitis (cases) and controls in a German discovery set and three replication sets. Functionally impaired variants were present in 29/944
Facile discovery of surrogate cytokine agonists.
Yen, et al.
Cell, 185, 1414-1430 (2023)
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Protocolli

Enzymatic Assay: Carboxypeptidase

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

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