Accéder au contenu
MilliporeSigma

C6423

α-Chymotrysin Protease

Cleaves at aromatic residues, suitable for mass spectrometry, from bovine pancreas

Se connecter pour consulter les tarifs organisationnels et contractuels.

Sélectionner une taille de conditionnement

Changer de vue

A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
eCl@ss:
42010112
NACRES:
NA.26
EC Number:
232-671-2
MDL number:
Numéro CE :
Service technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aider


Nom du produit

α-Chymotrypsin from bovine pancreas, suitable for protein sequencing, salt-free, lyophilized powder

grade

Proteomics Grade

Quality Level

form

salt-free, lyophilized powder

mol wt

25 kDa

suitability

suitable for protein sequencing

UniProt accession no.

storage temp.

2-8°C

Gene Information

cow ... CTRB1(618826)

General description

α-Chymotrypsin from bovine pancreas (bovine pancreatic α-chymotrypsin, CHT) is an enzyme protein. The influence of varying concentrations of organic solvents like ethanol, 1,4-dioxane and acetonitrile on CHT has been reported.
Chymotrypsin (Chy) is a serine protease. It corresponds to a molecular weight of 25.7 kDa and is widely used in pharmaceutical industry. It is synthesized in pancreas from chymotrypsinogen and require calcium for this conversion.

Application

α-Chymotrypsin from bovine pancreas is used for the following applications:
  • Protein Identification by mass spectrometry (MS)
  • The isolation and characterization of myosin heavy chains
  • Toxin preparation
  • The incubation of infected and uninfected cells for analysis of cellular proteins by SDS-PAGE
α-Chymotrypsin from bovine pancreas (BPC) may be used as a catalyst in the preparation of tetrahydroquinoline derivatives by Povarov reaction.

Biochem/physiol Actions

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.
α-Chymotrypsin from bovine pancreas is stabilized by Ca2+ and catalyzes the hydrolysis of peptide bonds in particular the amino acids tyrosine, phenylalanine, tryptophan, and leucine at their C-terminal side. α-Chymotrypsin is inhibited by Cu2+ and Hg.

Other Notes

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


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

Classe de stockage

11 - Combustible Solids

wgk

WGK 1

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves



Faites votre choix parmi les versions les plus récentes :

Certificats d'analyse (COA)

Lot/Batch Number

Vous ne trouvez pas la bonne version ?

Si vous avez besoin d'une version particulière, vous pouvez rechercher un certificat spécifique par le numéro de lot.

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents


Articles

Method development for protein fingerprinting of AAV serotype 5 using both intact mass analysis and peptide mapping, to determine critical quality attributes for gene therapy, utilizing three different columns.

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


Tessa E F Quax et al.
Virology, 404(1), 1-4 (2010-05-22)
Recently a unique mechanism of virion release was discovered in Archaea, different from lysis and egress systems of bacterial and eukaryotic viruses. It involves formation of pyramidal structures on the host cell surface that rupture the S-layer and by opening
A new platform for chymotrypsin isolation from fresh bovine pancreas using an environmental friendly polyelectrolyte: Alginate
Rausch C, et al.
BioChemistry: An Indian Journal, 9(6), 213-220 (2015)
L M Simon et al.
Biochemical and biophysical research communications, 280(5), 1367-1371 (2001-02-13)
The effects of different concentrations (20-95%) of organic solvents (ethanol, 1,4-dioxane and acetonitrile) were studied on alpha-chymotrypsin and trypsin from bovine pancreas. The changes in secondary structure were followed by CD measurements, and the apparent Michaelis constants (KMapp) and the



Numéro d'article de commerce international

RéférenceGTIN
C6423-.1MG04061832855981
C6423-25UG04061833511190