epitope corresponding to phosphorylated Ser 155 of Bad of human origin
recommended for detection of Ser 155 phosphorylated Bad of mouse origin, correspondingly phosphorylated Ser 118 of human origin and correspondingly phosphorylated Ser 156 of rat origin by WB, IP, IF and IHC(P)
p-Bad Background Information Phosphorylation of BAD, a pro-apoptotic member of the Bcl-2 protein family, on either serine 112 or serine 136 is thought to be necessary and sufficient for growth factors to promote cell survival (1–3). Serine 155 is a major site of phosphorylation by protein kinase A (PKA) and serum-induced kinases (1). Serine 155 phosphorylation requires the prior phosphorylation of serine 136, which recruits 14-3-3 proteins that then function to increase the accessibility of serine 155 to survival-promoting kinases (4). Like serine 112 and serine 136, phosphorylation of serine 155 inhibits the pro-apoptotic function of BAD (1). Serine 155 phosphorylation disrupts the binding of BAD to prosurvival Bcl-2 proteins and thereby promotes cell survival (4,5).
p-Bad (Ser 155) Références bibliographiques
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p-Bad (Ser 155)
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Western blot analysis of phosphorylated Bad expression in forskolin-treated 293 whole cell lysate (A,B). Blots were probed with p-Bad (Ser 155): sc-101641 (A) and p-Bad (Ser 155): sc-101641 preincubated with cognate phosphorylated peptide (B).
p-Bad (Ser 155): sc-101641. Immunoperoxidase staining of formalin-fixed, paraffin-embedded human breast carcinoma tissue extract showing cytoplasmic staining.
