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230790 Chymostatin - CAS 9076-44-2 - Calbiochem

Chymostatin, CAS 9076-44-2, is chymostatin “A” that specifically inhibits chymotrypsin (ID50 = 150 ng/ml), papain (ID50 = 7.5 µg/ml), and most cysteine proteases.

Chymostatin - CAS 9076-44-2 - Calbiochem : FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.

Synonymes: [(S)-1-Carboxy-2-phenylethyl]-carbamoyl-α-[2-amidohexahydro-4(S)-pyrimidyl]-(S)-glycyl-[A = Leu; B = Val; or C = Ile]-phenylalaninal

Primary Target: chymotrypsin
230790
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Aperçu

Replacement Information

Tableau de caractéristiques principal

CAS #Empirical Formula
9076-44-2C₂₅H₃₀N₆O₅X (X varies from lot to lot)

Products

RéférenceConditionnement Qté
230790-10MG Ampoule plast. 10 mg
230790-25MG Ampoule plast. 25 mg
230790-5MG Ampoule plast. 5 mg
Description
OverviewContains chymostatin "A" as a major form. Protease inhibitor produced by actinomycetes. Specifically inhibits chymotrypsin (ID50 = 150 ng/ml), papain (ID50 = 7.5 µg/ml), and most cysteine proteases.
M.W. 604 (avg.).
Catalogue Number230790
Brand Family Calbiochem®
Synonyms[(S)-1-Carboxy-2-phenylethyl]-carbamoyl-α-[2-amidohexahydro-4(S)-pyrimidyl]-(S)-glycyl-[A = Leu; B = Val; or C = Ile]-phenylalaninal
References
ReferencesMurakami, T., et al. 1991. Biochim. Biophys. Acta 1079, 279.
Umezawa, H. 1976. Methods Enzymol. 45, 678.
Product Information
CAS number9076-44-2
ATP CompetitiveN
FormWhite to slightly yellow solid or powder
Hill FormulaC₂₅H₃₀N₆O₅X (X varies from lot to lot)
Chemical formulaC₂₅H₃₀N₆O₅X (X varies from lot to lot)
ReversibleN
Quality LevelMQ100
Applications
ApplicationChymostatin, CAS 9076-44-2, is chymostatin “A” that specifically inhibits chymotrypsin (ID50 = 150 ng/ml), papain (ID50 = 7.5 µg/ml), and most cysteine proteases.
Biological Information
Primary Targetchymotrypsin
Primary Target IC<sub>50</sub>ID50 = 150 ng/ml, 7.5 µg/ml, against chymotrypsin, papain, respectively
Physicochemical Information
Cell permeableN
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
RTECSGC3047700
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage +2°C to +8°C
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Référence GTIN
230790-10MG 04055977218268
230790-25MG 04055977218275
230790-5MG 04055977218282

Documentation

Chymostatin - CAS 9076-44-2 - Calbiochem FDS

Titre

Fiche de données de sécurité des matériaux (FDS) 

Chymostatin - CAS 9076-44-2 - Calbiochem Certificats d'analyse

TitreNuméro de lot
230790

Références bibliographiques

Aperçu de la référence bibliographique
Murakami, T., et al. 1991. Biochim. Biophys. Acta 1079, 279.
Umezawa, H. 1976. Methods Enzymol. 45, 678.
Fiche technique

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision09-April-2018 JSW
Synonyms[(S)-1-Carboxy-2-phenylethyl]-carbamoyl-α-[2-amidohexahydro-4(S)-pyrimidyl]-(S)-glycyl-[A = Leu; B = Val; or C = Ile]-phenylalaninal
DescriptionMajor form is A. Protease inhibitor produced by actinomycetes. Specifically inhibits chymotrypsin, papain, and most cysteine proteases. Effective at concentrations = 10-100 µM.
FormWhite to slightly yellow solid or powder
CAS number9076-44-2
RTECSGC3047700
Chemical formulaC₂₅H₃₀N₆O₅X (X varies from lot to lot)
SolubilityDMSO (20 mg/ml), 5% glacial acetic acid (10 mg/ml)
Storage +2°C to +8°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.
Toxicity Standard Handling
ReferencesMurakami, T., et al. 1991. Biochim. Biophys. Acta 1079, 279.
Umezawa, H. 1976. Methods Enzymol. 45, 678.