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C9268
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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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
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
Related Categories
1 of 4
This Item | |||
|---|---|---|---|
| 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.
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Regulatory Listings
Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.
108-88-3
CAS No.
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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
Protocols
Carboxypeptidase A activity measured via continuous spectrophotometric rate determination assay with hippuryl-L-phenylalanine substrate.
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