|Other Accession||Q9Z272, Q68FF6|
|Other Names||ARF GTPase-activating protein GIT1, ARF GAP GIT1, Cool-associated and tyrosine-phosphorylated protein 1, CAT-1, CAT1, G protein-coupled receptor kinase-interactor 1, GRK-interacting protein 1, GIT1|
|Target/Specificity||The synthetic peptide sequence is selected from aa 381-395 of HUMAN GIT1|
|Format||Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.|
|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||GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes. Involved in the regulation of cytokinesis; the function may involve ENTR1 and PTPN13 (By similarity).|
|Cellular Location||Cytoplasm. Note=Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytoplasmic complexes and membrane protrusions. During cell migration, when cells detach, moves from the adhesions into the cytoplasmic complexes towards the leading edge, while, when cells adhere, it is found in vinculin-containing adhesions Recruitment to adhesions may be mediated by active tyrosine- phosphorylated paxillin|
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GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes (from SwissProt).
Kawachi, H., et al. Proc. Natl. Acad. Sci. U.S.A. 98(12):6593-6598(2001) Zhao, Z.S., et al. Mol. Cell. Biol. 20(17):6354-6363(2000) Premont, R.T., et al. J. Biol. Chem. 275(29):22373-22380(2000) Premont, R.T., et al. Proc. Natl. Acad. Sci. U.S.A. 95(24):14082-14087(1998)
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