C9268
Carboxypeptidase A aus Rinderpankreas
(Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution
Synonym(e):
Carboxypolypeptidase, Peptidyl-L-aminosäure-Hydrolase
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About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54
Empfohlene Produkte
Qualität
Proteomics Grade
(Type II-PMSF treated)
Qualitätsniveau
Form
ready-to-use solution
Spezifische Aktivität
≥50 units/mg protein
Mol-Gew.
~35 kDa
Aufgereinigt durch
2× crystallization
Verunreinigungen
≤0.05 BTEE units/mg protein chymotrypsin
≤10 BAEE units/mg protein trypsin
Lagertemp.
2-8°C
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Anwendung
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.
Biochem./physiol. Wirkung
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.
Einheitendefinition
One unit will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 at 25 °C.
Angaben zur Herstellung
Treated with phenylmethylsulfonyl fluoride to eliminate trypsin and chymotrypsin activity. Dialyzed and recrystallized: aqueous suspension with toluene added.
Hinweis zur Analyse
Protein determined by E1%/278
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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
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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
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Blood, 119(15), 3585-3594 (2012-03-01)
We used the opportunities afforded by the zebrafish to determine upstream pathways regulating mast cell development in vivo and identify their cellular origin. Colocalization studies demonstrated zebrafish notch receptor expression in cells expressing carboxypeptidase A5 (cpa5), a zebrafish mast cell-specific
Anne-Lise Marie et al.
Analytica chimica acta, 800, 103-110 (2013-10-15)
The present study describes a reproducible and quantitative capillary zone electrophoresis (CZE) method, which leads to the separation of nine forms (native, oxidized and glycated) of human serum albumin (HSA). In an attempt to identify the different species separated by
Protokolle
Enzymatic Assay of Carboxypeptidase
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