Phospho-Stathmin (Ser38) Antibody检测仅在Ser38位点磷酸化的内源性stathmin蛋白。通过人工合成人源stathmin蛋白Ser38位点周围相应的多肽片段去免疫动物从而制备出多克隆抗体。通过蛋白A和多肽亲和层析纯化抗体。Stathmin蛋白是一个广泛表达的微管不稳定的磷蛋白(phosphoprotein),该蛋白在许多癌症中被上调。该蛋白的氨基端包含多个磷酸化位点,并且涉及促进tubulin纤维解聚作用。这些位点的磷酸化使该蛋白失活和稳定微管。在G2/M期,通过CaM kinases II and IV(1,2)使Ser16位点磷酸化增加,并涉及有丝分裂纺锤体打的调节(3,4)。Ser38是cdc2激酶的靶蛋白 (5),并且TNF诱导的细胞死亡引起活性氧中间产物,这导致stathmin蛋白的过度磷酸化(6)。Rac和cdc42蛋白的EGF受体激活也增加stathmin蛋白在Ser16和Ser38位点的磷酸化(7)。其它紧密相关的家族成员是神经元性表达,并且包括SCG10、SCLIP、RB3和它的剪切体RB3'、RB3''。Stathmin和SCG10蛋白已经证明在PC12细胞神经样发育中起着一定作用(8)。
Phospho-Stathmin (Ser38) Antibody detects endogenous levels of stathmin protein only when phosphorylated at Ser38.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser38 of human stathmin. Antibodies are purified using protein A and peptide affinity chromatography.
Background
Stathmin is a ubiquitously expressed microtubule destabilizing phosphoprotein that is upregulated in a number of cancers. The amino terminus of the protein contains multiple phosphorylation sites and is involved in the promotion of tubulin filament depolymerization. Phosphorylation at these sites inactivates the protein and stabilizes microtubules. Ser16 phosphorylation by CaM kinases II and IV (1,2) increases during G2/M-phase and is involved in mitotic spindle regulation (3,4). Ser38 is a target for cdc2 kinase (5) and TNF-induced cell death gives rise to reactive oxygen intermediates leading to hyperphosphorylation of stathmin (6). EGF receptor activation of Rac and cdc42 also increases phosphorylation of stathmin on Ser16 and Ser38 (7). Other closely related family members are neuronally expressed and include SCG10, SCLIP, RB3 and its splice variants RB3' and RB3''. Stathmin and SCG10 have been shown to play roles in neuronal-like development in PC12 cells (8).