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217372 Carboxypeptidase Y, Excision Grade, Yeast

Carboxypeptidase Y, Excision Grade, Yeast : FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.
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Aperçu

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Description
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Native carboxypeptidase y from yeast. Serine protease that specifically cleaves C-terminal amino acids from proteins, with a preference for hydrophobic amino acids. Hydrolysis of C-terminal aspartic acid or glycine is very slow. Designed for the determination of C-terminal residues during protein sequencing.
Catalogue Number217372
Brand Family Calbiochem®
References
ReferencesStennicke, H.R., et al. 1994. Protein Eng. 7, 911.
Product Information
CAS number9046-67-7
Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol L-Ala from z-Phe-Ala per min at 37°C, pH 6.0.
EC number3.4.16.1
FormLyophilized
FormulationLyophilized from 50 mM sodium citrate, pH 6.0.
PI3.6
Applications
Biological Information
Purity≥90% by SDS-PAGE
Specific Activity≥300 units/mg protein
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage -20°C
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C) for long term storage or refrigerate (4°C ) for short term storage. Stock solutions are stable for up to 1 week at 4°C or for up to 1 month at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade ITEM Number
Référence GTIN
217372 0

Documentation

Carboxypeptidase Y, Excision Grade, Yeast Certificats d'analyse

TitreNuméro de lot
217372

Références bibliographiques

Aperçu de la référence bibliographique
Stennicke, H.R., et al. 1994. Protein Eng. 7, 911.
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.

Revision03-June-2008 RFH
DescriptionNative carboxypeptidase y from yeast. Serine protease that specifically cleaves C-terminal amino acids from proteins, with a preference for hydrophobic amino acids. Hydrolysis of C-terminal aspartic acid or glycine is very slow. Designed for the determination of C-terminal residues during protein sequencing.
FormLyophilized
FormulationLyophilized from 50 mM sodium citrate, pH 6.0.
Recommended reaction conditions1:100 (protease:protein by weight) for sequence analysis. Has an optimal pH of 5.5-6.5 and a pI of 3.6.
CAS number9046-67-7
EC number3.4.16.1
Purity≥90% by SDS-PAGE
Specific activity≥300 units/mg protein
Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol L-Ala from z-Phe-Ala per min at 37°C, pH 6.0.
SolubilityReconstitute in 50 µl of distilled H₂O.
Storage -20°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C) for long term storage or refrigerate (4°C ) for short term storage. Stock solutions are stable for up to 1 week at 4°C or for up to 1 month at -20°C.
Toxicity Standard Handling
ReferencesStennicke, H.R., et al. 1994. Protein Eng. 7, 911.

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Catégories

Life Science Research > Proteins and Enzymes > Other Enzymes