650277 Trypsin, Bovine, MS Grade

650277
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog Number AvailabilityPackaging Qty/Pack Price Quantity
      650277-1SET
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          Glass bottle 1 set
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          Description
          OverviewA chemically modified trypsin that is resistant to autolysis and degradation. Trypsin specifically hydrolyzes amides, peptides, and proteins at the C-terminus side of arginine and lysine residues. This mass spectrometry grade trypsin is methylated, TPCK treated, and affinity purified. It is specifically designed for digestion of proteins for sequencing and peptide fragment analysis by mass spectrometry. A trypsin to protein ratio of 1:100 to 1:20 is recommended for mass spectrometry protocols. Note: 1 SET = 5 X 20 µg of modified trypsin and 1 ml of resuspension buffer.
          Catalogue Number650277
          Brand Family Calbiochem®
          References
          ReferencesHenzel, W.J., et al. 1993. PNAS 90, 5011.
          Rice, R.H., et al. 1977. Biochim Biophys Acta 492, 316.
          Product Information
          Unit of DefinitionOne BAEE unit is defined as the ammount of enzyme required to produce a ΔA253 of 0.001 per min in a reaction volume of 3.2 ml at pH 7.6 at 25°C.
          FormLyophilized
          Applications
          Biological Information
          Specific Activity≥7500 BAEE U/mg
          Physicochemical Information
          ContaminantsChymostrypsin Activity: <3 BTEE U/mg (one BTEE unit is defined as the amount of enzyme required to hydrolyze 1 µmol BTEE per min at 25°C, pH 7.8.)
          Dimensions
          Materials Information
          Toxicological Information
          Safety Information according to GHS
          Safety Information
          R PhraseR: 36/37/38-42

          Irritating to eyes, respiratory system and skin.
          May cause sensitization by inhalation.
          S PhraseS: 22-24-26-36/37-45

          Do not breathe dust.
          Avoid contact with skin.
          In case of contact with eyes, rinse immediately with plenty of water and seek medical advice.
          Wear suitable protective clothing and gloves.
          In case of accident or if you feel unwell, seek medical advice immediately (show the label where possible).
          Product Usage Statements
          Storage and Shipping Information
          Ship Code Blue Ice Only
          Toxicity Multiple Toxicity Values, refer to MSDS
          Storage -20°C
          Do not freeze Ok to freeze
          Special InstructionsFollowing reconstitution, aliquot and freeze (-°C). Unused stock solutions are stable for up to 2 weeks at -70°C. Avoid freeze/thaw cycles of solution.
          Canadian export regulations Due to the country and/or U.S. state of origin of the animal material used in this product, this product may not be exported to Canada.
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          Trypsin, Bovine, MS Grade SDS

          Title

          Safety Data Sheet (SDS) 

          Trypsin, Bovine, MS Grade Certificates of Analysis

          TitleLot Number
          650277

          References

          Reference overview
          Henzel, W.J., et al. 1993. PNAS 90, 5011.
          Rice, R.H., et al. 1977. Biochim Biophys Acta 492, 316.
          Data Sheet

          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.

          Revision19-June-2009 JSW
          DescriptionA chemically modified trypsin that is resistant to autolysis and degradation. Trypsin specifically hydrolyzes amides, peptides, and proteins at the C-terminus side of arginine and lysine residues. This mass spectrometry grade trypsin is methylated, TPCK treated, and affinity purified. It is specifically designed for digestion of proteins for sequencing and peptide fragment analysis by mass spectrometry.
          FormLyophilized
          Recommended reaction conditions
          Materials Provided: • Trypsin, Bovine, MS Grade (Kit Component No. KP31814-20UG): 5 vials, 20 µg each • Trypsin Resuspension Buffer (Kit Component No. KP31815-0.5ML): 1 vial, 0.5 ml Preparation Before Use: Before opening the trypsin centrifuge the tube at 15,000 x g for 5 min. Suspend the MS Grade Trypsin in the Trypsin-Suspension Buffer. Recommended reconstitution concentration 0.5-1 µg/µl. IMPORTANT NOTE: In some cases, after reconstitution, there is insoluble material, which is a non-protein and will not interfere with trypsin activity. If you prefer to remove it, centrifuge the tube briefly and transfer the supernatant to a clean tube. Guidelines for use: For mass spectrometry sequence analysis, MS Grade Trypsin to protein ratio of 1:20 to 1:100 is recommended. Use freshly reconstituted MS Grade Trypsin in any sequence analysis. Any unused trypsin may be stored at -70°C and used within two weeks. Avoid repeated freeze-thaw cycle after re-suspension, which may lead to performance loss. Any available protocol can be used for digestion of proteins with MS Grade Bovine Trypsin.
          ContaminantsChymostrypsin Activity: <3 BTEE U/mg (one BTEE unit is defined as the amount of enzyme required to hydrolyze 1 µmol BTEE per min at 25°C, pH 7.8.)
          Specific activity≥7500 BAEE U/mg
          Unit definitionOne BAEE unit is defined as the ammount of enzyme required to produce a ΔA253 of 0.001 per min in a reaction volume of 3.2 ml at pH 7.6 at 25°C.
          Storage -20°C
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing reconstitution, aliquot and freeze (-°C). Unused stock solutions are stable for up to 2 weeks at -70°C. Avoid freeze/thaw cycles of solution.
          Toxicity Multiple Toxicity Values, refer to MSDS
          ReferencesHenzel, W.J., et al. 1993. PNAS 90, 5011.
          Rice, R.H., et al. 1977. Biochim Biophys Acta 492, 316.