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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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500 UNITS
119,00 €
2500 UNITS
402,00 €
5000 UNITS
436,00 €
Über diesen Artikel
CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥50 units/mg protein
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Unterstützung erhaltengrade
Proteomics Grade
Quality Level
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
Verwandte Kategorien
1 of 4
Dieser Artikel | |||
|---|---|---|---|
| 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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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
Zhenhua Li et al.
BMC bioinformatics, 13, 51-51 (2012-03-29)
Water is an integral part of protein complexes. It shapes protein binding sites by filling cavities and it bridges local contacts by hydrogen bonds. However, water molecules are usually not included in protein interface models in the past, and few
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
Protokolle
Carboxypeptidase A activity measured via continuous spectrophotometric rate determination assay with hippuryl-L-phenylalanine substrate.
Verwandter Inhalt
QC Methods
Global Trade Item Number
| SKU | GTIN |
|---|---|
| C9268-500UN | 04061833530429 |
| C9268-2.5KU | 04061832700403 |
| C9268-5KU | 04061833530436 |
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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?
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