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C3142

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

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

Sinônimo(s):

TLCK-Chymotrypsin

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About This Item

Número CAS:
9004-07-3
Número da licença da enzima:
3.4.21.1 (BRENDA, IUBMB)
Número CE:
232-671-2
Número MDL:
MFCD00130481
Código UNSPSC:
12352204
eCl@ss:
42010112
NACRES:
NA.54

tipo

Type VII

forma

essentially salt-free, lyophilized powder

atividade específica

≥40 units/mg protein

peso molecular

25 kDa

solubilidade

1 mM HCl: soluble 10 mg/mL, clear

nº de adesão UniProt

P00767

temperatura de armazenamento

−20°C

Informações sobre genes

cow ... CTRB1(618826)

Procurando produtos similares? Visita Guia de comparação de produtos

Aplicação

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.

Ações bioquímicas/fisiológicas

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.

Definição da unidade

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

Nota de preparo

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

Nota de análise

Protein determined by A1%/280

Outras notas

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

inibidor

Nº do produto
Descrição
Preços

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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

Aprotinina, lyophilized powder, 3-8 TIU/mg solid

P7626

Fluoreto de fenilmetanosulfonil, ≥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

substrato

Nº do produto
Descrição
Preços

Palavra indicadora

Danger

Classificações de perigo

Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Órgãos-alvo

Respiratory system

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 1

Equipamento de proteção individual

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

Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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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
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
Dhwani S Korde et al.
MethodsX, 9, 101779-101779 (2022-07-23)
Alzheimer´s disease is characterized by hyperphosphorylated tau neurofibrillary tangles and beta-amyloid plaques. Both molecules can be easily measured in human fluids or tissue extracts by immunoassays. However, the different molecular weight species can only be differentiated on Western Blot gels.
A Roussel et al.
The Journal of biological chemistry, 276(42), 38893-38898 (2001-08-10)
The crystal structures of two homologous inhibitors (PMP-C and PMP-D2v) from the insect Locusta migratoria have been determined in complex with bovine alpha-chymotrypsin at 2.1- and 3.0-A resolution, respectively. PMP-C is a potent bovine alpha-chymotrypsin inhibitor whereas native PMP-D2 is
Tobias Koschubs et al.
Nucleic acids research, 38(10), 3186-3195 (2010-02-04)
Mediator is the central coactivator complex required for regulated transcription by RNA polymerase (Pol) II. Mediator consists of 25 subunits arranged in the head, middle, tail and kinase modules. Structural and functional studies of Mediator are limited by the availability
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Chymotrypsin

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

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