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Key Documents

CHY5S

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

≥40 units/mg protein, vial of 5 mg

Sinônimo(s):

α-chymotrypsin A and B

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About This Item

Número CAS:
Número da licença da enzima:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

fonte biológica

bovine pancreas

Nível de qualidade

descrição

aseptically filled

tipo

Type IV-S

forma

solid

atividade específica

≥40 units/mg protein

peso molecular

25 kDa

composição

protein, ≥85% UV

embalagem

vial of 5 mg

nº de adesão UniProt

temperatura de armazenamento

−20°C

Informações sobre genes

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Aplicação

α-Chymotrypsin from bovine has been used in a study to inform proteasome inhibition in order to advance anticancer research. α-Chymotrypsin from bovine has also been used in a study that functionalized surface anchored poly(methylhydrosiloxane) thin films on oxidized silicon wafers.
α-Chymotrypsin from bovine pancreas has been used:
  • as a supplement for the collection of semen into Tris diluent
  • as one of the proteases in the analysis of major histocompatibility complex (MHC) class II protease sensitivity assay
  • as a component in YEPD broth for biofilm dispersion assay
  • in the preparation of chitinase–chymotrypsin–DMSO buffer (CCD buffer) for enzymatic digestion of larvae

The enzyme from Sigma has been used to assess the effect of limited proteolysis with α-chymotrypsin on the sperm penetration.

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, 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.

Definição da unidade

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

Nota de análise

Protein determined by A1%/280

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)

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Effect of enzyme treatment and mechanical removal of alpaca (Vicugna pacos) seminal plasma on sperm functional integrity
Morton K M, et al.
JOURNAL-SHANDONG UNIVERSITY OF SCIENCE AND TECHNOLOGY NATURAL SCIENCE, 5, 62-81 (2012)
A triad of molecular regions contribute to the formation of two distinct MHC class II conformers
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K L Honea et al.
Journal of assisted reproduction and genetics, 10(4), 255-260 (1993-05-01)
This study was designed to assess the impact of limited proteolysis with alpha-chymotrypsin on the sperm penetration assay (SPA) of infertile patients and to identify a group whose results would normalize with this pretreatment. Further, the application of this treatment
Immunofluorescent antibody staining of intact Drosophila larvae
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