This product contains HEPES buffer salts and a stabilizing carbohydrate component. The material may be reconstituted in water at 1mg/mL. Solution stability studies have not been performed, however, the stock solution is expected to be stable for 1 - 2 months when aliquoted and stored at −20°C. Avoid repeated freeze/thaw cycles. A datasheet is not available for this product. Please see the link below to review the enzyme assay protocol:
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/198/734/c9584enz.pdf
C9584
Carboxypeptidase B from porcine pancreas
lyophilized powder
Sinónimos:
Peptidyl-L-lysine(L-arginine) hydrolase, Protaminase
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| Tamaño de envase | SKU | Disponibilidad | Precio |
|---|---|---|---|
| 1 mg | Comprobar disponibilidad del carrito | $73.000 | |
| 5 mg | Comprobar disponibilidad del carrito | $251.000 |
$73.000
Comprobar disponibilidad del carrito
Servicio técnico
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Permítanos ayudarlebiological source
Porcine pancreas
Quality Level
grade
Proteomics Grade
form
lyophilized powder
specific activity
≥125 units/mg protein
mol wt
34,000 Da± 600
purified by
affinity chromatography
composition
Protein, 40-70%
foreign activity
carboxypeptidase A ≤1%, chymotrypsin ≤0.1%, trypsin ≤5%
storage temp.
−20°C
SMILES string
S(Cc3ccccc3)C(=O)C(NC(=O)C2N(CCC2)C(=O)C(NC(=O)C(NC(=O)CCC(=O)O)C)C)Cc1ccccc1
InChI
1S/C31H38N4O7S/c1-20(32-26(36)15-16-27(37)38)28(39)33-21(2)30(41)35-17-9-14-25(35)29(40)34-24(18-22-10-5-3-6-11-22)31(42)43-19-23-12-7-4-8-13-23/h3-8,10-13,20-21,24-25H,9,14-19H2,1-2H3,(H,32,36)(H,33,39)(H,34,40)(H,37,38)
InChI key
TWURVFFNODFJBJ-UHFFFAOYSA-N
Application
Carboxypeptidase B has been used in a study to develop a non-invasive pregnancy assay for use in both captive and wild polar bears. Carboxypeptidase B has been used in a study that identified new potential biomarkers of acute pancreatitis.
The enzyme from Sigma has been used to develop homogeneous time-resolved fluorescence (HTRF) assay for measuring carboxypeptidase B activity in a miniaturized high-throughput screening format.[1] It has been used to evaluate the impact of the C-terminal lysine(s) in human plasminogen binding to Bifidobacterium. The effect of treatment with carboxypeptidase B, which is a C-terminal lysine-specific endopeptidase, is measured using flow cytometry analysis.[2]
Biochem/physiol Actions
Carboxypeptidase B is a proteolytic enzyme capable of rapidly hydrolyzing peptide bonds to release certain carboxyl-terminal basic amino acids from peptides and proteins. Its molecular mass is 34,300±600 Da. It contains one non-dialyzable gram atom of zinc per mole. The enzyme activity is inhibited by metal chelating agents 1, 10-phenanthroline, 8-hydroxyquinoline-5-sulfonic acid, and 2,2′-dipyridyl.[3]
Packaging
Package size based on protein content
Physical form
Contains HEPES buffer salts, zinc chloride and carbohydrate
Preparation Note
Treated with protease inhibitor, AEBSF, to eliminate serine protease activity.
Analysis Note
Protein determined by biuret.
Other Notes
One unit will hydrolyze 1.0 μmole of hippuryl-L-arginine per min at pH 7.65 at 25 °C.
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Este artículo | |||
|---|---|---|---|
| grade Proteomics Grade | grade Proteomics Grade | grade - | grade - |
| biological source Porcine pancreas | biological source - | biological source - | biological source Porcine pancreas |
| specific activity ≥125 units/mg protein | specific activity ≥50 units/mg protein | specific activity ≥3 units/mg protein | specific activity ≥100 units/mg protein |
| form lyophilized powder | form ready-to-use solution | form lyophilized powder | form lyophilized |
| storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C | storage temp. −20°C |
| mol wt 34,000 Da± 600 | mol wt ~35 kDa | mol wt homodimer ~90 kDa | mol wt - |
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
wgk
WGK 3
ppe
Eyeshields, Gloves
Clase de almacenamiento
11 - Combustible Solids
flash_point_f
No data available
flash_point_c
No data available
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Contenido relacionado
QC Methods
Marc Ferrer et al.
Analytical biochemistry, 317(1), 94-98 (2003-05-06)
An epitope-unmasking, homogeneous time-resolved fluorescence (HTRF) assay has been developed for measuring carboxypeptidase B (CPB) activity in a miniaturized high-throughput screening format. The enzyme substrate (biotin-RYRGLMVGGVVR-OH) is cleaved by CPB at the C terminus, causing release of the C-terminal Arg
Andrew Lee et al.
Langmuir : the ACS journal of surfaces and colloids, 27(18), 11560-11574 (2011-08-13)
This article describes the use of capillary electrophoresis (CE) to examine the influence of different cations (C(+); C(+) = Na(+) and tetra-n-alkylammonium, NR(4)(+), where R = Me, Et, Pr, and Bu) on the rates of denaturation of bovine carbonic anhydrase
E Curry et al.
Theriogenology, 78(2), 308-314 (2012-04-28)
Currently, there is no method of accurately and non-invasively diagnosing pregnancy in polar bears. Specific proteins may exhibit altered profiles in the feces of pregnant bears, but predicting appropriate candidate proteins to investigate is speculative at best. The objective of
Número de artículo de comercio global
| SKU | GTIN |
|---|---|
| C9584-5MG | 04061833530900 |
| C9584-1MG | 04061833530894 |
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Chciałam zapytać jak przygotować roztwór Carboxypeptidase B from porcine, który występuje w postaci liofilizowanego proszku? Jest dostępna instrukcja?
1 answer-
Helpful?
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What is the Department of Transportation shipping information for this product?
1 answer-
Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
Helpful?
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Can Product C9584, Carboxypeptidase B from porcine pancreas be used to remove basic C-terminal residues of tryptic peptides?
1 answer-
The use of Product C9584, Carboxypeptidase B from porcine pancreas to remove basic C-terminal residues of tryptic peptides has been described in the literature. Please see the following as an example:The Protein Protocols Handbook, J.M. Walker, Ed., pp. 569, Humana Press, Totawa NJ (1996)
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