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Safety Information

C4129

Sigma-Aldrich

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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250 MG
CN¥768.76
500 MG
CN¥1,008.68
1 G
CN¥2,022.79
10 G
CN¥10,105.79

CN¥768.76

Available to ship onApril 16, 2025Details

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250 MG
CN¥768.76
500 MG
CN¥1,008.68
1 G
CN¥2,022.79
10 G
CN¥10,105.79

About This Item

CAS Number:
9004-07-3
Enzyme Commission number:
3.4.21.1 (BRENDA, IUBMB)
EC Number:
232-671-2
MDL number:
MFCD00130481
UNSPSC Code:
12352204
eCl@ss:
42010112
NACRES:
NA.54

CN¥768.76

Available to ship onApril 16, 2025Details

type

Type II

form

lyophilized powder

specific activity

≥40 units/mg protein

mol wt

25 kDa

composition

protein, ≥85%

color

white to off-white

UniProt accession no.

P00767

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

Gene Information

cow ... CTRB1(618826)

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1 of 4

This Item
C3142CHY5SC7762
α-Chymotrypsin from bovine pancreas Type II, lyophilized powder, ≥40 units/mg protein

C4129

α-Chymotrypsin from bovine pancreas

α-Chymotrypsin from bovine pancreas (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein

C3142

α-Chymotrypsin from bovine pancreas

α-Chymotrypsin from bovine pancreas ≥40 units/mg protein, vial of 5 mg

CHY5S

α-Chymotrypsin from bovine pancreas

α-Chymotrypsin from bovine pancreas Type I-S, essentially salt-free, lyophilized powder

C7762

α-Chymotrypsin from bovine pancreas

Gene Information

cow ... CTRB1(618826)

Gene Information

cow ... CTRB1(618826)

Gene Information

cow ... CTRB1(618826)

Gene Information

cow ... CTRB1(618826)

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

-

application(s)

-

form

lyophilized powder

form

essentially salt-free, lyophilized powder

form

solid

form

essentially salt-free, lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

Application

The enzyme from Sigma has been used to study the structure-function relationship in glycosylated α-chymotrypsin using immobilized metal-ion affinity chromatography (IMAC) and immobilized metal-ion affinity capillary electrophoresis (IMACE).[1]

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.

Unit Definition

One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

Preparation Note

Produced from 3× crystallized chymotrypsinogen

Analysis Note

Protein determined by E1%/280

Other Notes

View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer

Application

Product No.
Description
Pricing

inhibitor

Product No.
Description
Pricing

A2504

6-Aminocaproic acid, ≥99% (titration), powder

A7824

6-Aminocaproic acid, BioUltra, ≥99%

D0879

Diisopropylfluorophosphate

L2023

Leupeptin trifluoroacetate salt, ≥90% (HPLC), microbial

T9777

Trypsin-chymotrypsin inhibitor from Glycine max (soybean), lyophilized powder

A1153

Aprotinin from bovine lung, lyophilized powder, 3-8 TIU/mg solid

P7626

Phenylmethanesulfonyl fluoride, ≥98.5% (GC)

B1552

Bromoenol lactone, ≥98% (TLC)

A9024

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

A6150

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

A9285

α1-Antichymotrypsin from human plasma, ≥92.5% (SDS-PAGE), lyophilized powder

T4376

N-p-Tosyl-L-phenylalanine chloromethyl ketone, ≥97% (TLC), powder

C7268

Chymostatin, microbial

substrate

Product No.
Description
Pricing

Signal Word

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 Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

动植物源性产品
  • Specification Sheet

    • Choose from one of the most recent versions:

    Certificates of Analysis (COA)

    Lot/Batch Number
    0000422273
    0000422274
    0000422272
    0000422272
    0000422274

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    1. Which document(s) contains shelf-life or expiration date information for a given product?

      If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

    2. How do I get lot-specific information or a Certificate of Analysis?

      The lot specific COA document can be found by entering the lot number above under the "Documents" section.

    3. How do I find price and availability?

      There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

    4. What is the Department of Transportation shipping information for this product?

      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. 

    5. What is the molecular weight of alpha-chymotrypsin from bovine pancreas, product C4129?

      The molecular weight of alpha chymotrypsin, reported in the literature, is approximately 25 kDa.

    6. How do you recommend preparing a solution of Product No. C4129?

      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.

    7. How can solutions of alpha chymotrypsin (Product No. C4129) be stored?

      Stock solutions prepared in 1 mM HCl, containing 2 mM calcium chloride, can be stored at -20 ° for about one week.

    8. What is the pH optimum for the enzyme, Product No. C4129?

      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).

    9. My question is not addressed here, how can I contact Technical Service for assistance?

      Ask a Scientist here.

    Antonio Jesús Vizcaíno et al.
    Marine drugs, 18(6) (2020-06-24)
    This piece of research evaluates the presence of protease inhibitors in the macroalga Ulva ohnoi and provides an initial overview of their mode of action. The ability of Ulva protease inhibitors to inhibit digestive proteases of three marine fish species
    K Y Jiang et al.
    Biochimica et biophysica acta, 1433(1-2), 198-209 (1999-08-14)
    Chemical glycosylation of bovine alpha-chymotrypsin, by a glucosamine adduct on the carboxyl group, results in the modification of its catalytic activity. The structural alterations of alpha-chymotrypsin resulting from its glycosylation are studied by immobilized metal-ion affinity chromatography (IMAC) and immobilized
    Ines Atuh Ngoh et al.
    Experimental parasitology, 218, 107969-107969 (2020-08-29)
    Invasion of human red blood cells (RBCs) by Plasmodium parasites is a crucial yet poorly characterised phenotype. Two-color flow cytometry (2cFCM) promises to be a very sensitive and high throughput method for phenotyping parasite invasion. However, current protocols require high
    Olivia Ogilvie et al.
    MethodsX, 7, 101076-101076 (2020-10-10)
    Mass spectrometry (MS) is an emerging method to determine the accurate concentration of immunogenic gluten peptides. It is of interest to quantify specific peptides within the gluten peptidome due to the role they play in the activation of the celiac
    Shannon Gwala et al.
    Food & function, 11(3), 2509-2521 (2020-03-07)
    Postharvest storage of legumes is a strategy to ensure food security. However, the hard-to-cook phenomenon, partly explained by pectin-cation-phytate theory, may develop during storage. Based on this theory, minerals could be redistributed within the matrix, affecting the concentration of free/bound
    View All Related Papers

    Articles

    Chymotrypsin

    Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

    Protocols

    Procedure for Enzymatic Assay of α-Chymotrypsin (EC 3.4.21.1)

    Follow our procedure for the determination of a chymotrypsin activity. This enzymatic assay of alpha chymotrypsin guides you through the entire process and necessary calculations.

    Chromatograms

    application for HPLC

    Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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