It is recommended to reconstitute Product No. C4129 in 1 mM hydrochloric acid containing 2 mM calcium chloride. The calcium functions as a stabilizer, and possibly an activator, of the enzyme.
C4129
α-Chymotrypsin from bovine pancreas
Type II, lyophilized powder, ≥40 units/mg protein
Synonyme(s) :
α-chymotrypsin A and B, alpha-chymotrypsin
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250 MG
71.40 CHF
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110.00 CHF
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198.00 CHF
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1 280.00 CHF
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Type II
Niveau de qualité
Forme
lyophilized powder
Activité spécifique
≥40 units/mg protein
Poids mol.
25 kDa
Composition
protein, ≥85%
Couleur
white to off-white
Numéro d'accès UniProt
Application(s)
diagnostic assay manufacturing
Température de stockage
−20°C
Informations sur le gène
cow ... CTRB1(618826)
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Catégories apparentées
1 of 4
Cet article | C7762 | C6423 | 230900 |
|---|---|---|---|
| Gene Information cow ... CTRB1(618826) | Gene Information cow ... CTRB1(618826) | Gene Information cow ... CTRB1(618826) | Gene Information - |
| specific activity ≥40 units/mg protein | specific activity ≥40 units/mg protein | specific activity - | specific activity - |
| form lyophilized powder | form essentially salt-free, lyophilized powder | form salt-free, lyophilized powder | form lyophilized |
| application(s) diagnostic assay manufacturing | application(s) - | application(s) - | application(s) - |
| UniProt accession no. | UniProt accession no. | UniProt accession no. | UniProt accession no. - |
| storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C |
Application
The enzyme from Sigma has been used to study the structure-function relationship in glycosylated α-chymotrypsin using immobilized metal-ion affinity chromatography (IMAC) and immobilized metal-ion affinity capillary electrophoresis (IMACE).[1]
Actions biochimiques/physiologiques
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. The 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.
Notes préparatoires
Produced from 3× crystallized chymotrypsinogen
Remarque sur l'analyse
Protein determined by E1%/280
Autres remarques
One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer
Produit(s) apparenté(s)
Réf. du produit
Description
Tarif
used together
Réf. du produit
Description
Tarif
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Organes cibles
Respiratory system
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Équipement de protection individuelle
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Antonio Jesús Vizcaíno et al.
Marine drugs, 18(6) (2020-06-24)
This piece of research evaluates the presence of protease inhibitors in the macroalga Ulva ohnoi and provides an initial overview of their mode of action. The ability of Ulva protease inhibitors to inhibit digestive proteases of three marine fish species
Ines Atuh Ngoh et al.
Experimental parasitology, 218, 107969-107969 (2020-08-29)
Invasion of human red blood cells (RBCs) by Plasmodium parasites is a crucial yet poorly characterised phenotype. Two-color flow cytometry (2cFCM) promises to be a very sensitive and high throughput method for phenotyping parasite invasion. However, current protocols require high
K Y Jiang et al.
Biochimica et biophysica acta, 1433(1-2), 198-209 (1999-08-14)
Chemical glycosylation of bovine alpha-chymotrypsin, by a glucosamine adduct on the carboxyl group, results in the modification of its catalytic activity. The structural alterations of alpha-chymotrypsin resulting from its glycosylation are studied by immobilized metal-ion affinity chromatography (IMAC) and immobilized
Shannon Gwala et al.
Food & function, 11(3), 2509-2521 (2020-03-07)
Postharvest storage of legumes is a strategy to ensure food security. However, the hard-to-cook phenomenon, partly explained by pectin-cation-phytate theory, may develop during storage. Based on this theory, minerals could be redistributed within the matrix, affecting the concentration of free/bound
Olivia Ogilvie et al.
MethodsX, 7, 101076-101076 (2020-10-10)
Mass spectrometry (MS) is an emerging method to determine the accurate concentration of immunogenic gluten peptides. It is of interest to quantify specific peptides within the gluten peptidome due to the role they play in the activation of the celiac
Articles
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
Protocoles
Follow our procedure for the determination of a chymotrypsin activity. This enzymatic assay of alpha chymotrypsin guides you through the entire process and necessary calculations.
Contenu apparenté
QC Methods
Chromatograms
application for HPLC
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How do you recommend preparing a solution of Product No. C4129?
1 answer-
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What is the Department of Transportation shipping information for this product?
1 answer-
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.
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How can solutions of alpha chymotrypsin (Product No. C4129) be stored?
1 answer-
Stock solutions prepared in 1 mM HCl, containing 2 mM calcium chloride, can be stored at -20 ° for about one week.
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What is the pH optimum for the enzyme, Product No. C4129?
1 answer-
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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What is the molecular weight of alpha-chymotrypsin from bovine pancreas, product C4129?
1 answer-
The molecular weight of alpha chymotrypsin, reported in the literature, is approximately 25 kDa.
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