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324713 Endoproteinase Glu-C, Excision Grade, Staphylococcus aureus

324713
Purchase on Sigma-Aldrich

Descripción

Replacement Information

Products

Número de referenciaEmbalaje Cant./Env.
324713-50UG Frasco de vidrio 50 μg
Description
OverviewNative endoproteinase Glu-C from Staphylococcus aureus. Serine protease that specifically hydrolyzes peptide bonds at the carboxylic side of glutamic acid and aspartic acid residues. Inhibited by DFP and α2-macroglobulin. Suggested working concentration: 1:20 to 1:100 (protease:protein by weight) for sequence analysis.
Catalogue Number324713
Brand Family Calbiochem®
SynonymsV8 Protease
References
ReferencesHoumard, J., and Drapeau, G.R. 1972. Proc. Natl. Acad. Sci. USA 69, 3506.
Product Information
CAS number66676-43-5
Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol Z-Phe-Leu-Glu-<i>p</i>NA per min at 25°C, pH 7.8.
EC number3.4.21.19
FormLyophilized
Quality LevelMQ100
Applications
Biological Information
Specific Activity≥10 units/mg protein
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
R PhraseR: 20-36/37/38-42/43

Harmful by inhalation.
Irritating to eyes, respiratory system and skin.
May cause sensitization by inhalation and skin contact.
S PhraseS: 22-26-36

Do not breathe dust.
In case of contact with eyes, rinse immediately with plenty of water and seek medical advice.
Wear suitable protective clothing.
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Harmful
Storage +2°C to +8°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 2 days at 4°C or for up to 1 month at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Número de referencia GTIN
324713-50UG 07790788049171

Documentation

Endoproteinase Glu-C, Excision Grade, Staphylococcus aureus Ficha datos de seguridad (MSDS)

Título

Ficha técnica de seguridad del material (MSDS) 

Endoproteinase Glu-C, Excision Grade, Staphylococcus aureus Certificados de análisis

CargoNúmero de lote
324713

Referencias bibliográficas

Visión general referencias
Houmard, J., and Drapeau, G.R. 1972. Proc. Natl. Acad. Sci. USA 69, 3506.
Ficha técnica

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.

Revision13-September-2024 JSW
SynonymsV8 Protease
DescriptionNative endoproteinase Glu-C from Staphylococcus aureus. Serine protease that specifically hydrolyzes peptide bonds at the carboxylic side of glutamic acid and aspartic acid residues. Inhibited by DFP and α2-macroglobulin.
FormLyophilized
Recommended reaction conditions
Protocol 1. Dissolve the protein to be digested in buffer (e.g. 25 mM ammonium carbonate, pH 7.8). If the protein requires denaturation, add SDS (≤0.1%), guanidine hydrochloride (≤1 M), or urea (≤1 M) to the digestion buffer. (Note: if urea is used, also include 20 mM methylamine to avoid cyanate ion blockage of the N-terminus substrate protein. 2. Suggested working concentration is 1:20-1:100 (protease:protein by weight for sequence analysis). 3. Incubate for 2-18 h at 25°C.
CAS number66676-43-5
EC number3.4.21.19
Specific activity≥10 units/mg protein
Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol Z-Phe-Leu-Glu-pNA per min at 25°C, pH 7.8.
SolubilityH₂O
Storage +2°C to +8°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 2 days at 4°C or for up to 1 month at -20°C.
Toxicity Harmful
ReferencesHoumard, J., and Drapeau, G.R. 1972. Proc. Natl. Acad. Sci. USA 69, 3506.

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Categorías

Life Science Research > Proteins and Enzymes > Other Enzymes