|Other Names||Transient receptor potential cation channel subfamily M member 7, Channel-kinase 1, Long transient receptor potential channel 7, LTrpC-7, LTrpC7, TRPM7, CHAK1, LTRPC7|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8052a was selected from the N-term region of human CHAK1 . 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||Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. Involved in TNF- induced necroptosis downstream of MLKL by mediating calcium influx. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1).|
|Cellular Location||Membrane; Multi-pass membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
TRPCs, mammalian homologs of the Drosophila transient receptor potential (trp) protein, are ion channels that are thought to mediate capacitative calcium entry into the cell. TRP-PLIK is a protein that is both an ion channel and a kinase. As a channel, it conducts calcium and monovalent cations to depolarize cells and increase intracellular calcium. As a kinase, it is capable of phosphorylating itself and other substrates. The kinase activity is necessary for channel function, as shown by its dependence on intracellular ATP and by the kinase mutants.[supplied by OMIM]
Blume-Jensen P, et al. Nature 2001. 411: 355.Cantrell D, J. Cell Sci. 2001. 114: 1439.Jhiang S Oncogene 2000. 19: 5590.Manning G, et al. Science 2002. 298: 1912.Moller, D, et al. Am. J. Physiol. 1994. 266: C351-C359.Robertson, S. et al. Trends Genet. 2000. 16: 368.Robinson D, et al. Oncogene 2000. 19: 5548.Van der Ven, P, et al. Hum. Molec. Genet. 1993. 2: 1889.Vanhaesebroeck, B, et al. Biochem. J. 2000. 346: 561.Van Weering D, et al. Recent Results Cancer Res. 1998. 154: 271.
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