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539480 Proteinase K, Tritirachium album

Proteinase K, Tritirachium album MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
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539480
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Overview

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539480-100MGCN
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      539480-25MGCN
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          Description
          OverviewSerine protease that exhibits strong proteolytic activity on a wide variety of denatured and native proteins of high molecular weight. Because of its rapid proteolytic inactivation of endogenous nucleases, it can be used for isolation of mRNA and high molecular weight DNA. Preferentially cleaves bonds next to the carbonyl group of N-substituted hydrophobic, aliphatic, and aromatic amino acids. Inhibited by DFP, Hg2+, and PMSF. Not inactivated by metal chelators, sulfhydryl reagents, TLCK, or TPCK.
          Catalogue Number539480
          Brand Family Calbiochem®
          References
          ReferencesWatazu, Y., et al. 1993. J. Lab. Clin. Anal. 7, 81.
          Lebherz, H.G., et al. 1986. Biochem. J. 233, 51.
          Ebeling, W., et al. 1974. Eur. J. Biochem. 47, 91.
          Product Information
          CAS number39450-01-6
          Activity≥30 mAnsonU/mg dry weight
          Unit of DefinitionOne mAnson unit is defined as the amount of enzyme that will liberate 1.0 µmol of Folin-positive amino acids (calculated as tyrosine) per min at 37°C, pH 7.5.
          EC number3.4.21.14
          FormWhite lyophilized solid
          FormulationLyophilized from calcium acetate
          Quality LevelMQ300
          Applications
          Biological Information
          Specific Activity≥40 mAnsonU/mg protein
          Physicochemical Information
          ContaminantsDNase: no detectable nicking activity with pBR322, incubation for 6 h at 37°C; RNase: no ribonuclease activity with MS2 RNA detected after incubation for 6 h at 37°C
          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 Irritant
          Storage +2°C to +8°C
          Do not freeze Ok to freeze
          Special InstructionsFollowing reconstitution, store in the refrigerator (4°C). Stock solutions prepared in 50 mM Tris-HCl, 2 mM calcium acetate, pH 8.0 are stable for up to 1 year at 4°C.
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications
          Global Trade Item Number
          Catalogue Number GTIN
          539480-100MGCN 04055977269147
          539480-25MGCN 07790788051327

          Documentation

          Proteinase K, Tritirachium album SDS

          Title

          Safety Data Sheet (SDS) 

          Proteinase K, Tritirachium album Certificates of Analysis

          TitleLot Number
          539480

          References

          Reference overview
          Watazu, Y., et al. 1993. J. Lab. Clin. Anal. 7, 81.
          Lebherz, H.G., et al. 1986. Biochem. J. 233, 51.
          Ebeling, W., et al. 1974. Eur. J. Biochem. 47, 91.

          Brochure

          Title
          Bulk Product Guide
          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.

          Revision16-November-2016 JSW
          DescriptionSerine protease that exhibits strong proteolytic activity on a wide variety of denatured and native proteins of high molecular weight. Because of its rapid proteolytic inactivation of endogenous nucleases, it can be used for isolation of mRNA and high molecular weight DNA. Preferentially cleaves bonds next to the carbonyl group of N-substituted hydrophobic, aliphatic, and aromatic amino acids. Inhibited by DFP, Hg2+, and PMSF. Not inactivated by metal chelators, sulfhydryl reagents, TLCK, or TPCK.
          FormWhite lyophilized solid
          FormulationLyophilized from calcium acetate
          Recommended reaction conditions

          Anson Enzyme Activity Assay: Materials Required • 5 ml of Hemoglobin (20 mg/ml) in 100 mM phosphate buffer, pH 7.5 (6 M urea, 5 mM NaCl). • 0.6 ml of 20 mM CaCl2 dissolved in distilled water. • 0.1 ml of proteinase K (40 µg/ml) in 20 mM CaCl2 Activity Assay Protocol 1. Mix the 5 ml hemoglobin, 0.6 ml CaCl2, and 0.1 ml proteinase K and make up the volume to 6 ml with 20 mM CaCl2; incubate for 10 min at 25°C. 2. Add 10 ml 300 mM Trichloroacetic acid and incubate at room temperature for 30 min. 3. Centrifuge and transfer 5 ml of the supernatant to a clean tube. Add 10 ml 500 mM NaOH and 3 ml Folin reagent (diluted 1:2 with redistilled water); incubate for 5 min at room temperature. 4. Measure the ΔA at 750 nm. For calibration use tyrosine solutions. 1 mAnson unit liberates 1 µmole of Folin-positive amino acids per min (calculated as tyrosine) under test conditions.
          CAS number39450-01-6
          EC number3.4.21.14
          ContaminantsDNase: no detectable nicking activity with pBR322, incubation for 6 h at 37°C; RNase: no ribonuclease activity with MS2 RNA detected after incubation for 6 h at 37°C
          Specific activity≥40 mAnsonU/mg protein
          Activity≥30 mAnsonU/mg dry weight
          Unit definitionOne mAnson unit is defined as the amount of enzyme that will liberate 1.0 µmol of Folin-positive amino acids (calculated as tyrosine) per min at 37°C, pH 7.5.
          Solubility50 mM Tris-HCl, 2 mM calcium acetate, pH 8.0
          Storage +2°C to +8°C
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing reconstitution, store in the refrigerator (4°C). Stock solutions prepared in 50 mM Tris-HCl, 2 mM calcium acetate, pH 8.0 are stable for up to 1 year at 4°C.
          Toxicity Irritant
          ReferencesWatazu, Y., et al. 1993. J. Lab. Clin. Anal. 7, 81.
          Lebherz, H.G., et al. 1986. Biochem. J. 233, 51.
          Ebeling, W., et al. 1974. Eur. J. Biochem. 47, 91.