208712
Calpain-1, Porcine Erythrocytes
Calpain-1, Porcine Erythrocytes, is a native calpain-1. A heterodimeric cysteine proteinase with low Ca2+ requirement (EC₅₀ = 2 µM).
Synonym(s):
μ-Calpain
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General description
Native 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.
Native 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.
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.
Packaging
Please refer to vial label for lot-specific concentration.
Warning
Toxicity: Harmful (C)
Unit Definition
One 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
Physical form
In 20 mM imidazole-HCl, 5 mM β-mercaptoethanol, 1 mM EDTA, 1 mM EGTA, 30% glycerol, pH 6.8.
Reconstitution
Following initial thaw, aliquot and freeze (-70°C). Short-term storage of aliquots at 4°C or on ice is not recommended.
Other Notes
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. Neurotrauma14, 121.
Johnson, G.V.W., and Gutmann, R.P. 1997. BioEssays19, 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. USA90, 2628.
Goll, D.E., et al. 1992. BioEssays14, 549.
Ishii, H., et al. 1992. Biochim. Biophys. Acta1175, 37.
Melloni, E., and Pontremoli, S. 1989. Trends Neurosci.12, 438.
Ross, E., and Schatz, G. 1973. Anal. Biochem.54, 304.
Sorimachi, H., et al. 1997. Biochem. J.328, 721.
Kampfl, A., et al. 1997. J. Neurotrauma14, 121.
Johnson, G.V.W., and Gutmann, R.P. 1997. BioEssays19, 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. USA90, 2628.
Goll, D.E., et al. 1992. BioEssays14, 549.
Ishii, H., et al. 1992. Biochim. Biophys. Acta1175, 37.
Melloni, E., and Pontremoli, S. 1989. Trends Neurosci.12, 438.
Ross, E., and Schatz, G. 1973. Anal. Biochem.54, 304.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Certificates of Analysis (COA)
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