208712 | Calpain-1, Porcine Erythrocytes

208712
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      208712-1MG
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      Stocked 
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          Plastic ampoule 1 mg
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          Description
          OverviewNative calpain-1 from porcine erythrocytes. Ca2+-dependent heterodimeric cysteine proteinase with low Ca2+ requirement (EC50= 2 µM). Participates in the ATP release reaction of platelets stimulated with thrombin.
          Catalogue Number208712
          Brand Family Calbiochem®
          Synonymsμ-Calpain
          References
          ReferencesVanderklish, P.W., and Bahr, B.A. 2000. Int. J. Exp. Pathol. 81, 323.
          Sorimachi, H., et al. 1997. Biochem. J. 328, 721.
          Kampfl, A., et al. 1997. J. Neurotrauma 14, 121.
          Johnson, G.V.W., and Gutmann, R.P. 1997. BioEssays 19, 1011.
          Bartus, R.T., et al. 1995. Neurol. Res. 17, 249.
          Wang, K.K.W., and Yuen, P.-W. 1994. Trends Pharmacol. Sci. 15, 412.
          Saito, K., et al. 1993. Proc. Natl. Acad. Sci. USA 90, 2628.
          Goll, D.E., et al. 1992. BioEssays 14, 549.
          Ishii, H., et al. 1992. Biochim. Biophys. Acta 1175, 37.
          Melloni, E., and Pontremoli, S. 1989. Trends Neurosci. 12, 438.
          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 pmol Suc-LLVY-AMC in 1 min at 25°C using the Calpain Activity Assay Kit, Fluorogenic (Cat. No. QIA120). Note: 1 caseinolytic unit = 9 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.
          PI5.3
          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
          208712

          References

          Reference overview
          Vanderklish, P.W., and Bahr, B.A. 2000. Int. J. Exp. Pathol. 81, 323.
          Sorimachi, H., et al. 1997. Biochem. J. 328, 721.
          Kampfl, A., et al. 1997. J. Neurotrauma 14, 121.
          Johnson, G.V.W., and Gutmann, R.P. 1997. BioEssays 19, 1011.
          Bartus, R.T., et al. 1995. Neurol. Res. 17, 249.
          Wang, K.K.W., and Yuen, P.-W. 1994. Trends Pharmacol. Sci. 15, 412.
          Saito, K., et al. 1993. Proc. Natl. Acad. Sci. USA 90, 2628.
          Goll, D.E., et al. 1992. BioEssays 14, 549.
          Ishii, H., et al. 1992. Biochim. Biophys. Acta 1175, 37.
          Melloni, E., and Pontremoli, S. 1989. Trends Neurosci. 12, 438.
          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
          Synonymsμ-Calpain
          DescriptionNative calpain-1 from porcine erythrocytes. Calpains are a family of calcium-dependent thiol-proteases that degrade 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. Over-activation 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. Over-expression 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 pmol Suc-LLVY-AMC in 1 min at 25°C using the Calpain Activity Assay Kit, Fluorogenic (Cat. No. QIA120). Note: 1 caseinolytic unit = 9 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
          ReferencesVanderklish, P.W., and Bahr, B.A. 2000. Int. J. Exp. Pathol. 81, 323.
          Sorimachi, H., et al. 1997. Biochem. J. 328, 721.
          Kampfl, A., et al. 1997. J. Neurotrauma 14, 121.
          Johnson, G.V.W., and Gutmann, R.P. 1997. BioEssays 19, 1011.
          Bartus, R.T., et al. 1995. Neurol. Res. 17, 249.
          Wang, K.K.W., and Yuen, P.-W. 1994. Trends Pharmacol. Sci. 15, 412.
          Saito, K., et al. 1993. Proc. Natl. Acad. Sci. USA 90, 2628.
          Goll, D.E., et al. 1992. BioEssays 14, 549.
          Ishii, H., et al. 1992. Biochim. Biophys. Acta 1175, 37.
          Melloni, E., and Pontremoli, S. 1989. Trends Neurosci. 12, 438.
          Ross, E., and Schatz, G. 1973. Anal. Biochem. 54, 304.

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          Categories

          Life Science Research > Proteins and Enzymes > Other Enzymes