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[anti-HA]
Regulation of the PI3-K/Akt Survival Pathway in the Rat Endometrium Biol Reprod, Mar 2013; 88: 79.
[Akt3]
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[LA]
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[JAK2]
A phospho-specific peptide corresponding to residues surrounding S916 were used as an immunogen. This antibody detects PKC mu phosphorylated on Serine 916.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
PKC mu is a novel member of the subgroup of atypical protein kinase Cs (PKC). Deduced protein sequence shows strong homology to conserved domains of members of the PKC subfamily. In vitro phorbol ester binding studies and kinase assays with lysates of cells overexpressing PKC mu showed phorbol ester-independent kinase activity, autophosphorylation, and, in normal rat kidney (NRK) cells, predominant phosphorylation of a 30-kDa protein at serine residues. Data suggest a role of PKC mu in signal transduction pathways related to growth control (1). PKC mu is a cytosolic protein, which upon binding to the trans-Golgi network (TGN) regulates the fission of transport carriers specifically destined to the cell surface. (2). Results demonstrate that betagamma subunits of the heterotrimeric G proteins directly activates PKD by interacting with its pleckstrin homology domain (3).
Related Pathway
EGFR1 Signaling Pathway
Wnt Signaling Pathway
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Western blot analysis on HeLa cell lysates using anti-Phospho-PKC mu/PKD (p916), 1:100,000 dilution. Cells were either (A) untreated (B) treated with TPA.
