|Other Names||Presequence protease, mitochondrial, hPreP, 3424-, Pitrilysin metalloproteinase 1, Metalloprotease 1, hMP1, PITRM1, KIAA1104, MP1|
|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||Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing (PubMed:10360838, PubMed:16849325, PubMed:19196155, PubMed:24931469). Has an ATP-independent activity (PubMed:16849325). Specifically cleaves peptides in the range of 5 to 65 residues (PubMed:19196155). Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference (PubMed:10360838, PubMed:19196155, PubMed:24931469). Degrades the transit peptides of mitochondrial proteins after their cleavage (PubMed:19196155). Also degrades other unstructured peptides (PubMed:19196155). It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion (PubMed:16849325, PubMed:24931469). It is a highly efficient protease, at least toward amyloid-beta protein 40 (PubMed:24931469). Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently (PubMed:24931469).|
|Cellular Location||Mitochondrion matrix|
|Tissue Location||Widely expressed. Expressed at higher level in muscle and heart compared to brain, pancreas, liver, lung and placenta.|
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Provided below are standard protocols that you may find useful for product applications.
ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Able to degrade amyloid beta A4 (APP) protein when it accumulates in mitochondrion, suggesting a link with Alzheimer disease. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference.
Yoshida, T., et al. Int. J. Mol. Med. 25(4):649-656(2010)Pinho, C.M., et al. Neurosci. Lett. 469(2):204-208(2010)Oguri, M., et al. Am. J. Hypertens. 23(1):70-77(2010)Yoshida, T., et al. Int. J. Mol. Med. 24(4):539-547(2009)Chow, K.M., et al. Biochemistry 48(13):2868-2877(2009)
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