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C3142

α-Chymotrypsin from bovine pancreas

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

Synonym(s):

TLCK-Chymotrypsin

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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
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Quality Level

type

Type VII

form

essentially salt-free, lyophilized powder

specific activity

≥40 units/mg protein

mol wt

25 kDa

solubility

1 mM HCl: soluble 10 mg/mL, clear

UniProt accession no.

storage temp.

−20°C

Gene Information

cow ... CTRB1(618826)

Application

α-Chymotrypsin from Sigma has been used to determine the crystal structures of two homologous inhibitors (pars intercerebralis major peptide-C and pars intercerebralis major peptide-D2v) from the insect Locusta migratoria by forming a complex with the enzyme.[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. Its 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, 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

TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.

Analysis Note

Protein determined by A1%/280

Other Notes

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

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CHY5SC7762C4879
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 solid

form

essentially salt-free, lyophilized powder

form

solid

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

solubility

1 mM HCl: soluble 10 mg/mL, clear

solubility

-

solubility

1 mM HCl: soluble 2.0 mg/mL, clear

solubility

1 mM HCl: soluble 10 mg/mL, clear, colorless

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

mol wt

25,656 Da by calculation


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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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Product Information Sheet


M Gestin et al.
Digestive diseases and sciences, 42(6), 1302-1311 (1997-06-01)
A specific method for pancreatic elastase II activity analysis was developed. True elastase II activity could be discriminated from that of elastase I and chymotrypsin. The postnatal development of four pancreatic proteases in the duodenal juice of children and in
Zhenyao Luo et al.
FEBS letters, 592(13), 2341-2350 (2018-06-02)
The bacterium Streptococcus pneumoniae (the pneumococcus) is a major human pathogen that requires Zn2+ for its survival and virulence in the host environment. Polyhistidine triad protein D (PhtD) has a known role in pneumococcal Zn2+ homeostasis. However, the mechanistic basis
Tommi Kotila et al.
Nature communications, 13(1), 3442-3442 (2022-06-16)
Actin polymerization generates forces for cellular processes throughout the eukaryotic kingdom, but our understanding of the 'ancient' actin turnover machineries is limited. We show that, despite > 1 billion years of evolution, pathogenic Leishmania major parasite and mammalian actins share the same



Global Trade Item Number

SKUGTIN
C3142-25MG04061833485460
C3142-10MG04061833485453
C3142-100MG04061833485446

Questions

1–5 of 5 Questions  
  1. How do you recommend preparing a solution of Product No. C3142?

    1 answer
    1. It is recommended to reconstitute Product No. C3142 in 1 mM hydrochloric acid containing 2 mM calcium chloride. The calcium functions as both a stabilizer (and possibly an activator) of the enzyme.

      Helpful?

  2. What is the molecular weight of alpha-chymotrypsin from bovine pancreas (Product No. C3142)?

    1 answer
    1. 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) at our website.

      Helpful?

  3. How can solutions of alpha-chymotrypsin (Product No. C3142) be stored?

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

      Helpful?

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

    1 answer
    1. 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?

  5. What is the pH optimum for the enzyme, Product No. C3142?

    1 answer
    1. 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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