Phospho-Progesterone Receptor (Ser345) Antibody

• 产品编号：CST-12783S      品牌：CST       原厂货号：12783S
• 产品分类：抗体 > 一抗 > 磷酸化抗体
• 应用分类：

描述：

只有当丝氨酸（345和181位）磷酸化时，Phospho-Progesterone Receptor (Ser345) Antibody能够分别识别内源性水平的孕酮受体B（PR-B）和孕酮受体A（PR-A）蛋白。该抗体不与其他孕酮受体家族成员发生交叉反应。该多克隆抗体通过用合成磷酸肽免疫动物制备，该合成磷酸肽是人孕酮受体蛋白B（PR-B）蛋白丝氨酸（345位）附近的残基。抗体由蛋白A和肽亲和层析纯化。人孕酮受体（PR）表现为两种形式：全长的孕酮受体B和短的孕酮受体A。PR A缺少PR B的第164个氨基酸残基（1,2）。PR A和PR B都是配体激活，但其激活靶基因转录的相对能力是不同的（3,4）。PR的活性受磷酸化调节。在其氨基末端区域，至少有七个丝氨酸残基被磷酸化。丝氨酸三个位点（81，102，162位）是全长PR特有的，而其他丝氨酸位点（190，294，345和400位）是两个亚型所共有的（5）。PR B丝氨酸（190位）（相当于PR A丝氨酸（26位））的磷酸化是由CDK2催化的(6)。丝氨酸（190位）的突变导致PR活性降低(7)，这表明丝氨酸（190位）的磷酸化对其生物功能来说是至关重要的。研究表明PR-B丝氨酸（345位）的配体依赖性磷酸化由MAPK催化，在介导乳腺癌细胞的增殖中起着重要的作用。调查表明，PR-B 丝氨酸（345位）的磷酸化与Sp1有关，调控EGFR和p21的转录（8）。

1. Evans, R.M. (1988) Science 240, 889-895.
2. Kastner, P. et al. (1990) EMBO J. 112, 1603-1614.
3. Giangrande, P.H. et al. (2000) Mol. Cell. Biol. 20, 3102-3115.
4. Wen, D.X. et al. (1994) Mol. Cell. Biol. 14, 8356-8364.
5. Clemm, D.L. et al. (2000) Mol. Endocrinol. 14, 52-65.
6. Zhang, Y. et al. (1997) Mol. Endocrinol. 11, 823-832.
7. Takimoto, G.S. et al. (1996) J. Biol. Chem. 271, 13308-13316.
8. Faivre, E.J. et al. (2008) Mol Endocrinol 22, 823-37.

原厂资料：

Specificity / Sensitivity

Phospho-Progesterone Receptor (Ser345) Antibody recognizes endogenous levels of progesterone receptor B (PR-B) and progesterone receptor A (PR-A) proteins only when phosphorylated at Ser345 and Ser181, respectively. This antibody does not cross-react with other progesterone receptor family members.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser345 of human progesterone receptor B (PR-B) protein. Antibodies are purified by protein A and peptide affinity chromatography.

Background

Human progesterone receptor (PR) is expressed as two forms: the full length PR-B and the short form PR-A. PR-A lacks the first 164 amino acid residues of PR-B (1,2). Both PR-A and PR-B are ligand activated, but differ in their relative ability to activate target gene transcription (3,4). The activity of PR is regulated by phosphorylation; at least seven serine residues are phosphorylated in its amino-terminal domain. Three sites (Ser81, Ser102, and Ser162) are unique to full length PR-B, while other sites (Ser190, Ser294, Ser345, and Ser400) are shared by both isoforms (5). Phosphorylation of PR-B at Ser190 (equivalent to Ser26 of PR-A) is catalyzed by CDK2 (6). Mutation of Ser190 results in decreased activity of PR (7), suggesting that the phosphorylation at Ser190 may be critical to its biological function.

1. Evans, R.M. (1988) Science 240, 889-895.
2. Kastner, P. et al. (1990) EMBO J. 112, 1603-1614.
3. Giangrande, P.H. et al. (2000) Mol. Cell. Biol. 20, 3102-3115.
4. Wen, D.X. et al. (1994) Mol. Cell. Biol. 14, 8356-8364.
5. Clemm, D.L. et al. (2000) Mol. Endocrinol. 14, 52-65.
6. Zhang, Y. et al. (1997) Mol. Endocrinol. 11, 823-832.
7. Takimoto, G.S. et al. (1996) J. Biol. Chem. 271, 13308-13316.
8. Faivre, E.J. et al. (2008) Mol Endocrinol 22, 823-37.

注意事项：

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM
NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C.
Do not aliquot the antibody.