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Native endoproteinase Asp-N from Pseudomonas fragi. Designed for protein sequencing or sequence verification, analysis of protein structural domains, and cleavage of fusion proteins. Metalloprotease that specifically hydrolyzes proteins at the N-terminal side of aspartic acid and cysteic acid residues. Inhibited by aprotinin, DFP, leupeptin, and TLCK. Suggested working concentration: 1:20 to 1:100 (protease:protein by weight) for sequence analysis.
Catalogue Number
324708
Brand Family
Calbiochem®
References
References
Drapeau, G.R. 1980. J. Biol. Chem.255, 839.
Product Information
CAS number
9001-92-7
Unit of Definition
One unit is defined as the amount of enzyme that will release a sufficient amount of azo dye from AZOCOLL™ Substrate (Cat. No. 194932) to produce an increase in absorbance at 520 nm of 0.001 per min at 37°C, pH 7.5.
Harmful by inhalation. Irritating to eyes, respiratory system and skin. May cause sensitization by inhalation and skin contact.
S Phrase
S: 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 Instructions
Following 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.
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.
Revision
19-June-2008 RFH
Description
Native endoproteinase Asp-N from Pseudomonas fragi. Designed for protein sequencing or sequence verification, analysis of protein structural domains, and cleavage of fusion proteins. Metalloprotease that specifically hydrolyzes proteins and the N-terminal side of aspartic acid and cysteic acid residues. Inhibited by aprotinin, DFP, leupeptin, and TLCK.
Form
White lyophilized solid
Formulation
Lyophilized from 10 mM Tris-HCl, pH 7.5.
Recommended reaction conditions
Protocol
1. Reconstitute in 50 µl of distilled H2O.
2. Dissolve the proteins to be sequenced in phosphate, acetate, or Tris buffer, pH 6.0-8.5. For proteins that are difficult to solubilize, add urea (up to 1 M), SDS (0.01%), or guanidine-HCl (up to 1 M) to the digestion buffer.
3. Use a 1:20-1:100 ratio of proteinase to protein by weight for sequence analysis.
4. Incubate between 2-18 h at 37°C. Incubation time is dependent on the amount of enzyme used.
CAS number
9001-92-7
EC number
3.4.24.33
Purity
≥90% by SDS-PAGE
Specific activity
≥20,000 units/mg protein
Unit definition
One unit is defined as the amount of enzyme that will release a sufficient amount of azo dye from AZOCOLL™ Substrate (Cat. No. 194932) to produce an increase in absorbance at 520 nm of 0.001 per min at 37°C, pH 7.5.
Solubility
H₂O
Storage
+2°C to +8°C
Do Not Freeze
Ok to freeze
Special Instructions
Following 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.
