Phospho-PKD/PKC mu (Ser916)抗体识别内源性的Ser916磷酸化的PKD1/PKC mu。此抗体在某些物种中可能与PKD2亚型有交叉反应。该多克隆抗体用与小鼠PKD中Ser916位点附近的氨基酸序列对应的人工合成磷酸化的肽段免疫动物而制成。该抗体使用蛋白A和蛋白亲和层析纯化而得。
Phospho-PKD/PKC mu (Ser916) Antibody detects endogenous levels of PKD1/PKC mu only when phosphorylated at serine 916. Ths antibody may also cross-react with isoform PKD2, in some species.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser916 of mouse PKD. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Activation of PKC is one of the earliest events in a cascade leading to a variety of cellular responses such as secretion, gene expression, proliferation and muscle contraction (1,2). Protein kinase D (PKD), also called PKCμ, is a serine/threonine kinase whose activation is dependent on the phosphorylation of two activation loop sites, Ser744 and Ser748, via a PKC-dependent signaling pathway (3-5). In addition to the two activation loop sites, the carboxy-terminal Ser916 has been identified as an autophosphorylation site for PKD/PKCμ. Phosphorylation at Ser916 correlates with PKD/PKCμ catalytic activity (6).
Background
Activation of PKC is one of the earliest events in a cascade leading to a variety of cellular responses such as secretion, gene expression, proliferation and muscle contraction (1,2). Protein kinase D (PKD), also called PKCμ, is a serine/threonine kinase whose activation is dependent on the phosphorylation of two activation loop sites, Ser744 and Ser748, via a PKC-dependent signaling pathway (3-5). In addition to the two activation loop sites, the carboxy-terminal Ser916 has been identified as an autophosphorylation site for PKD/PKCμ. Phosphorylation at Ser916 correlates with PKD/PKCμ catalytic activity (6).