|Other Names||Myotubularin-related protein 1, Phosphatidylinositol-3-phosphate phosphatase, Mtmr1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6801a was selected from the N-term region of human MTMR1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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||Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol (3,5)-bisphosphate.|
|Cellular Location||Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm|
|Tissue Location||Widely expressed. Detected in skeletal muscle, heart, lung, liver and brain.|
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MTM1 gene mutations cause X-linked myotubular myopathy. The corresponding protein, myotubularin, contains the consensus active site of tyrosine phosphatases (PTP) and is a tyrosine/serine phosphatase. The 3.7-kb MTMR1 mRNA is expressed ubiquitously. An additional 3.1-kb transcript was detected only in placenta. Analysis of the genomic region containing MTM1 and MTMR1 reveals that the 2 genes share a similar structure, suggesting that they are related and arose from an intrachromosomal gene duplication. The 2 main MTMR1 protein muscular isoforms, like myotubularin, dephosphorylate PI(3)P in vitro. There is a striking reduction in the level of the muscle-specific isoform and the appearance of an abnormal MTMR1 transcript in cultured differentiated muscle cells and in skeletal muscle from congenital myotonic dystrophy patients. MTMR1 may play a role in muscle formation, and may represent another target for abnormal mRNA splicing in myotonic dystrophy.
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).Laporte, J., et al., Hum. Mol. Genet. 7(11):1703-1712 (1998).
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