The Calcium concentration in most classical medium formulations, including RPMI, is sufficient to activate and/or stabilize α-Chymotrypsin.
α-Chymotrypsin calcium requirements:
Significant occupancy of Ca2+ site - approximately 0.1 mM
Saturating level - approximately 1 mM
Concentration for stock solution storage - 5–10 mM
Please see the link below to review additional information available in the TLCK-treated version of this product, C3142:
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/349/963/c3142pis.pdf
C4129
α-Chymotrypsin from bovine pancreas
Type II, lyophilized powder, ≥40 units/mg protein
Synonym(s):
α-chymotrypsin A and B, alpha-chymotrypsin
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| Size/SKU | Availability | Price |
|---|---|---|
250 mg | Available to ship onSeptember 29, 2026fromMILWAUKEE | $88.90 |
500 mg | Available to ship onSeptember 29, 2026fromMILWAUKEE | $179.00 |
1 g | Available to ship onSeptember 29, 2026fromMILWAUKEE | $526.00 |
10 g | Estimated to ship onOctober 13, 2026fromMILWAUKEE | $2,500.00 |
About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
42010112
EC Number:
232-671-2
NACRES:
NA.54
MDL number:
EC Number:
Specific activity:
≥40 units/mg protein
$88.90
Available to ship onSeptember 29, 2026Details
type
Type II
Quality Segment
form
lyophilized powder
specific activity
≥40 units/mg protein
mol wt
25 kDa
composition
protein, ≥85%
color
white to off-white
UniProt accession no.
application(s)
diagnostic assay manufacturing
storage temp.
−20°C
Gene Information
cow ... CTRB1(618826)
Application
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, 10 mM 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
Produced from 3× crystallized chymotrypsinogen
Analysis Note
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 II, lyophilized powder, ≥40 units/mg protein | description Type I-S, essentially salt-free, lyophilized powder | description suitable for protein sequencing, salt-free, lyophilized powder | description (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein |
| 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 - | specific activity ≥40 units/mg protein |
| application(s) diagnostic assay manufacturing | application(s) - | application(s) - | application(s) - |
| form lyophilized powder | form essentially salt-free, lyophilized powder | form salt-free, lyophilized powder | form essentially salt-free, lyophilized powder |
| UniProt accession no. | UniProt accession no. | UniProt accession no. | UniProt accession no. |
| storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C |
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Signal Word
Danger
Hazard Codes
Precautionary Statements
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
PPE (personal protective equipment)
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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I intend to use it in RPMI cell conditioned media which I read contains at least ~0.5 mM Ca. Is this sufficient?
1 answer-
Helpful?
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What is the pH optimum for the enzyme, Product No. C4129?
1 answer-
The pH optimum for alpha-chymotrypsin is between pH 7.5-8.5. Please see the following reference: Wilcox, P.E., Chymotrypsingogens-chymotrypsins, Methods in Enzymology, 19, 64-80 (1970).
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What is the molecular weight of alpha-chymotrypsin from bovine pancreas, product C4129?
1 answer-
The molecular weight of alpha chymotrypsin, reported in the literature, is approximately 25 kDa.
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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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How can solutions of alpha chymotrypsin (Product No. C4129) be stored?
1 answer-
Stock solutions prepared in 1 mM HCl, containing 2 mM calcium chloride, can be stored at -20 ° for about one week.
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How do you recommend preparing a solution of Product No. C4129?
1 answer-
It is recommended to reconstitute Product No. C4129 in 1 mM hydrochloric acid containing 2 mM calcium chloride. The calcium functions as a stabilizer, and possibly an activator, of the enzyme.
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