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
C9268
Carboxypeptidase A from bovine pancreas
(Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution
동의어(들):
Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase
조직 및 계약 가격을 보려면 로그인를 클릭합니다.
크기 선택
보기 변경
| 사이즈/SKU | 재고 정보 | 가격 (VAT 별도) |
|---|---|---|
500 units | 구입 가능 여부는 고객센터에 문의하십시오. | ₩242,991 |
2500 units | 구입 가능 여부는 고객센터에 문의하십시오. | ₩536,428 |
5000 units | 구입 가능 여부는 고객센터에 문의하십시오. | ₩872,393 |
제품정보 (DICE 배송 시 비용 별도)
CAS 번호:
UNSPSC Code:
12352204
NACRES:
NA.54
EC 번호:
MDL number:
Specific activity:
≥50 units/mg protein
grade
Proteomics Grade
Quality Segment
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
Application
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.
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.
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.
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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이 품목 | |||
|---|---|---|---|
| description (Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution | description (Type II-PMSF treated), ≥20 units/mg protein | description ammonium sulfate suspension, ≥6 units/mL packed gel, 25 °C, enzyme from bovine pancreas | description lyophilized powder |
| grade Proteomics Grade | grade - | grade - | grade Proteomics Grade |
| specific activity ≥50 units/mg protein | specific activity ≥20 units/mg protein | specific activity ≥6 units/mL packed gel, 25 °C | specific activity ≥125 units/mg protein |
| form ready-to-use solution | form aqueous suspension | form ammonium sulfate suspension | form lyophilized powder |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. −20°C |
| mol wt ~35 kDa | mol wt ~35 kDa | mol wt ~35,250 | mol wt 34,000 Da± 600 |
| Quality Level 300 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
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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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