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C6423

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

suitable for protein sequencing, salt-free, lyophilized powder

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About This Item

Numer CAS:
9004-07-3
Numer EC enzymu:
3.4.21.1 (BRENDA, IUBMB)
Numer WE:
232-671-2
Numer MDL:
MFCD00130481
Kod UNSPSC:
12352204
eCl@ss:
42010112
NACRES:
NA.26

klasa czystości

Proteomics Grade

Poziom jakości

200

Postać

salt-free, lyophilized powder

masa cząsteczkowa

25 kDa

przydatność

suitable for protein sequencing

numer dostępu UniProt

P00767

temp. przechowywania

2-8°C

informacje o genach

cow ... CTRB1(618826)

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Opis ogólny

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.

Zastosowanie

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.

Działania biochem./fizjol.

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.
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.

Definicja jednostki

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

Inne uwagi

View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer
This page may contain text that has been machine translated.

inhibitor

Numer produktu
Opis
Cennik

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

substrat

Numer produktu
Opis
Cennik

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

H302,H315,H319,H334,H335,H400

Klasyfikacja zagrożeń

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

Organy docelowe

Respiratory system

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 1

Środki ochrony indywidualnej

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

Certyfikaty analizy (CoA)

Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.

Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
S Herrero et al.
Applied and environmental microbiology, 67(3), 1085-1089 (2001-03-07)
Susceptibility to protoxin and toxin forms of Cry1Ab and the binding of (125)I-labeled Cry1Ab and Cry1Ac has been examined in three Plodia interpunctella colonies, one susceptible (688(s)) and two resistant (198(r) and Dpl(r)) to Bacillus thuringiensis. Toxicological studies showed that
Xinyu Liu et al.
eLife, 9 (2020-12-05)
The production of reactive oxygen species (ROS) is a ubiquitous defense response in plants. Adapted pathogens evolved mechanisms to counteract the deleterious effects of host-derived ROS and promote infection. How plant pathogens regulate this elaborate response against ROS burst remains
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Produkty

Chymotrypsyna

Enzym analityczny Chymotrypsyna: Chymotrypsyna jest wytwarzana w komórkach gruczołowych trzustki jako nieaktywny prekursor, chymotrypsynogen.

Chymotrypsin

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

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