Hip Antibody识别内源性的全部Hip蛋白。该多克隆抗体用与人类Hip蛋白氨基酸序列对应的人工合成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。Hip (Hsc70互作蛋白)蛋白也被称为ST13(肿瘤生成蛋白抑制物13),是若干共分子伴侣之一,可以调节HSP70分子伴侣家族的活性(1,2)。同源寡聚蛋白Hip在蛋白折叠中通过稳定HSP70的ADP结合状态与HSP70协同作用。当HSP70被HSP40家族转化为ADP结合状态时,Hip直接结合到HSP70的ATP酶结构域(3)。与其它正性共刺激因子如HSP40和Hop协调作用,或者与负性共刺激因子如Bag1竞争,Hip能促进HSP70在蛋白折叠和修复中的分子伴侣功能,并且能够控制调节性蛋白如固醇受体和多种增殖或凋亡相关的调节因子(4-8)。
Hip Antibody detects endogenous levels of total Hip protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to human Hip. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).