|Other Names||ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial, CLPX|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex (PubMed:11923310, PubMed:22710082). Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure (PubMed:22841477). ATP- dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through upregulation of heme biosynthesis (PubMed:25957689).|
|Cellular Location||Mitochondrion. Mitochondrion matrix, mitochondrion nucleoid|
|Tissue Location||Higher expression in skeletal muscle and heart and to a lesser extent in liver, brain, placenta, lung, kidney and pancreas.|
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ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of clpP (By similarity).
Martin, A., et al. Mol. Cell 29(4):441-450(2008)Bogenhagen, D.F., et al. J. Biol. Chem. 283(6):3665-3675(2008)Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :Kang, S.G., et al. J. Biol. Chem. 280(42):35424-35432(2005)Kang, S.G., et al. J. Biol. Chem. 277(23):21095-21102(2002)
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