Background: Activation of protein kinase C is a key signal transduction event in mesangial cell dedifferentiation and proliferation, yet little is known about downstream substrates or their roles in normal or diseased states. SSeCKS, a novel protein kinase C substrate originally isolated as a src-suppressed negative mitogenic regulator in fibroblasts, controls actinbased cytoskeletal architecture and scaffolds key signaling kinases such as protein kinase C and protein kinase A. Activation of protein kinase C is a key signal transduction event in mesangial cell dedifferentiation. A role for SSeCKS, a PKA/PKC scaffolding protein, has been implicated during the process of spermiogenesis and in the actin-based stellate morphology of mesangial cells
Positive Control: Rat aortic smooth muscle
Purification Method: Ammonium Sulfate Precipitation
Concentration: See vial for concentration
Source: Sheep were immunized with a recombinant protein corresponding to amino acids 620-1596 of the SSeCKS protein.
References: 1. Lin, X., et al. 'A novel src- and ras-suppressed protein kinase C substrate with cytoskeletal architecture.' J. Biol. Chem. 1996, 271, 28430-284382. Siegel, S.M., et al. 'SSeCKS immunolabeling in rat primary sensory neurons.' Brain Res. 2002, 926, 126-1363. Nelson, P.J., et al. 'Involvement of the protein kinase C substrate, SSeCKS, in the actin-based stellate morphology of mesangial cells.' J. Cell. Sci. 1999, 112, 361-370
UniProt: Q62766 (Rat)
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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