208715 Calpain-2, Porcine Kidney

208715
  
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      Overview

      Replacement Information

      Key Spec Table

      Description
      OverviewNative calpain-2 from porcine kidney. Ca2+-dependent heterodimeric cysteine proteinase with high Ca2+ requirement (EC50 = 1 mM). The Ca2+ requirement for proteolysis of nuclear matrix proteins is dramatically decreased in the presence of DNA.

      This product has been discontinued.





      Catalogue Number208715
      Brand Family Calbiochem®
      Synonymsm-Calpain
      References
      ReferencesKampfl, A., et al. 1997. J. Neurotrauma 14, 121.
      Sorimachi, H., et al. 1997. Biochem. J. 328, 721.
      Mellgren, R.L., et al. 1993. J. Biol. Chem. 268, 653.
      Ross, E., and Schatz, G. 1973. Anal. Biochem. 54, 304.
      Product Information
      Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 pmol Suc-LLVY-AMC in 1 min, 25°C using the Calpain Activity Assay Kit, Fluorogenic (Cat. No. QIA120). 1 caseinolytic unit = 7 fluorogenic units.
      EC number3.4.22.17
      FormLiquid
      FormulationIn 20 mM imidazole-HCl, 5 mM β-mercaptoethanol, 1 mM EDTA, 1 mM EGTA, 30% glycerol, pH 6.8.
      PI4.6
      Applications
      Biological Information
      Specific Activity≥1000 units/mg protein
      Concentration Label Please refer to vial label for lot-specific concentration
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      R PhraseR: 36/37/38-42/43

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

      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 Dry Ice Only
      Toxicity Harmful
      Storage ≤ -70°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C). Short-term storage of aliquots at 4°C or on ice is not recommended.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      SDS

      Title

      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      208715

      References

      Reference overview
      Kampfl, A., et al. 1997. J. Neurotrauma 14, 121.
      Sorimachi, H., et al. 1997. Biochem. J. 328, 721.
      Mellgren, R.L., et al. 1993. J. Biol. Chem. 268, 653.
      Ross, E., and Schatz, G. 1973. Anal. Biochem. 54, 304.

      Brochure

      Title
      Calcium Metabolism and Related Products Brochure
      Proteases Technical Bulletin
      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.

      Revision18-May-2010 JSW
      Synonymsm-Calpain
      DescriptionNative calpain-2 from porcine kidney. Calpains are a family of calcium-dependent thiol-proteases that proteolyze a wide variety of cytoskeletal, membrane associated, and regulatory proteins. The two major isoforms, calpain I (µ-form) and calpain II (m-form), differ in their calcium requirement for activation. Calpain I requires only micromolar amounts of calcium (EC50 = 2 µM), while calpain II requires millimolar amounts (EC50 = 1 mM).

      Calpains are heterodimers of 80 kDa and 30 kDa subunits. The 80 kDa unit has the catalytic site and is unique to each isozyme. The 30 kDa unit is a regulatory subunit and common to both calpain I and calpain II. The 80 kDa unit consists of four domains (I-IV). The 30 kDa unit has two domains (V and VI).

      • Domain I is partially removed during autolysis.
      • Domain II is the protease domain.
      • Domain III exhibits a homology with typical calmodulin binding proteins and interacts with calcium binding domains (IV and VI) and frees domain II for protease activity.
      • Domain IV is a calcium binding domain.
      • Domain V contains a hydrophobic region and is essential for calpain interaction with membranes.
      • Domain VI is a calcium binding domain.

      More recently, attention has been focused on the pathological significance of calcium accumulation in the central nervous system following cerebral ischemia and traumatic brain injury. Overactivation of NMDA, kainate, and AMPA receptors in the brain leads to sustained influx in Ca2+ through voltage gated Ca2+ channels. Disturbances in calcium homeostasis result in the activation of several calcium-dependent enzymes including calpains. Overexpression of calpains has been positively linked to both acute and chronic neurodegenerative processes including ischemia, trauma, and Alzheimer's disease. In Alzheimer's disease the ratio of active (76 kDa) to inactive (80 kDa) calpain I is reported to be much higher. Calpain proteolysis is usually the late-stage common pathway towards cell death induced by excitotoxic compounds.
      FormLiquid
      FormulationIn 20 mM imidazole-HCl, 5 mM β-mercaptoethanol, 1 mM EDTA, 1 mM EGTA, 30% glycerol, pH 6.8.
      Concentration Label Please refer to vial label for lot-specific concentration
      EC number3.4.22.17
      Specific activity≥1000 units/mg protein
      Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 pmol Suc-LLVY-AMC in 1 min, 25°C using the Calpain Activity Assay Kit, Fluorogenic (Cat. No. QIA120). 1 caseinolytic unit = 7 fluorogenic units.
      Storage ≤ -70°C
      Avoid freeze/thaw
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C). Short-term storage of aliquots at 4°C or on ice is not recommended.
      Toxicity Harmful
      ReferencesKampfl, A., et al. 1997. J. Neurotrauma 14, 121.
      Sorimachi, H., et al. 1997. Biochem. J. 328, 721.
      Mellgren, R.L., et al. 1993. J. Biol. Chem. 268, 653.
      Ross, E., and Schatz, G. 1973. Anal. Biochem. 54, 304.

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      Categories

      Life Science Research > Proteins and Enzymes > Other Enzymes