It is recommended to reconstitute product C7762 in 1 mM hydrochloric acid containing 2 mM calcium chloride. The calcium functions as both a stabilizer (and possibly an activator) of the enzyme.
C7762
α-Chymotrypsin from bovine pancreas
Type I-S, essentially salt-free, lyophilized powder
Synonym(s):
α-chymotrypsin A and B, alpha-chymotrypsin
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| Size/SKU | Availability | Price |
|---|---|---|
5 mg | Available to ship TODAYfromMILWAUKEE | $69.10 |
25 mg | Available to ship TODAYfromMILWAUKEE | $97.30 |
100 mg | Available to ship TODAYfromMILWAUKEE | $272.00 |
About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
42010112
EC Number:
232-671-2
NACRES:
NA.54
MDL number:
Specific activity:
≥40 units/mg protein
$69.10
Available to ship TODAYDetails
type
Type I-S
Quality Segment
form
essentially salt-free, lyophilized powder
specific activity
≥40 units/mg protein
mol wt
25 kDa
purified by
3× crystallization
solubility
1 mM HCl: soluble 2.0 mg/mL, clear
UniProt accession no.
storage temp.
−20°C
Gene Information
cow ... CTRB1(618826)
Application
The product has been used to investigate the inhibitory effect of several ether oligomers against the enzyme. It has also been used to cleave pro-phenoloxidase in order to estimate total phenoloxidase in haemolymph. Furthermore, the enzyme has been used as a positive control in chymotrypsin assays using salivary gland and anterior midgut extracts of Deraeocoris nigritulus.
α-Chymotrypsin from bovine pancreas has been used in a study to investigate protein extraction by Winsor-III microemulsion systems. α-Chymotrypsin from bovine pancreas has also been used in a study to investigate a new specific fullerene-based fluorescent probe for trypsin.
Biochem/physiol Actions
α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. The pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, as well as 10 mM of Cu2+ and Hg2+.
A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.
Preparation Note
Prepared free of autolysis products and low molecular weight contaminants.
The powder may be reconstituted in 1 mM HCl at 2 mg/mL concentration to form a clear solution.
Analysis Note
Minimum 85% protein
Protein determined by E1%/280
Other Notes
One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer
1 of 1
This Item | |||
|---|---|---|---|
| description Type I-S, essentially salt-free, lyophilized powder | description Type II, lyophilized powder, ≥40 units/mg protein | description (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein | description ≥40 units/mg protein, vial of 5 mg |
| Gene Information cow ... CTRB1(618826) | Gene Information cow ... CTRB1(618826) | Gene Information cow ... CTRB1(618826) | Gene Information cow ... CTRB1(618826) |
| specific activity ≥40 units/mg protein | specific activity ≥40 units/mg protein | specific activity ≥40 units/mg protein | specific activity ≥40 units/mg protein |
| form essentially salt-free, lyophilized powder | form lyophilized powder | form essentially salt-free, lyophilized powder | form solid |
| solubility 1 mM HCl: soluble 2.0 mg/mL, clear | solubility - | solubility 1 mM HCl: soluble 10 mg/mL, clear | solubility - |
| UniProt accession no. | UniProt accession no. | UniProt accession no. | UniProt accession no. |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
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signalword
Danger
Hazard Classifications
Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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How should I prepare a solution of α-Chymotrypsin, Product C7762?
1 answer-
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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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What is the molecular weight of alpha-chymotrypsin from bovine pancreas (Product No. C7762)?
1 answer-
The molecular weight of alpha chymotrypsin, reported in the literature, is approximately 25 kDa. This information and the basic structure description of the enzyme can be found on our product information sheet (under Documents, above).
Helpful?
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How can solutions of α-Chymotrypsin, Product C7762, be stored?
1 answer-
Stock solutions prepared in 1 mM HCl, containing 2 mM calcium chloride can be stored at -20 °C for about one week.
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What is the pH optimum for the enzyme, α-Chymotrypsin, Product C7762?
1 answer-
The pH optimum is between pH 7.5-8.5.
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