The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress. It includes cytoplasmic (Hsp90-alpha/beta), ER (Grp94) and mitochondrial (TRAP1) localized members. Hsp90 is structurally composed of an N-terminal ATP binding domain, a medial substrate-binding region, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones to stabilize a multitude of client protein substrates. TRAP1 (aka Hsp75) was originally identified as a chaperone binding partner for retinoblastoma protein. TRAP1 was later found by immunofluorescence to be localized to the mitochondria. TRAP1 is significantly more active as an ATPase due in part to the lack of regulatory elements in the C-terminus, but retains the ability to dimerize. However, it does not form stable complexes with typical cochaperones of Hsp90 like p23 and HOP4. TRAP1 has been identified as a protective element for cell survival, and has been suggested as a target for anti-cancer therapeutics.
应用类型
WB
免疫原
Recombinant human TRAP1.
来源宿主
Rabbit
反应性
该Anti-TRAP1 抗体的反应性请参考该产品的说明书
保存建议
Long term storage at -20C. Avoid freeze/thaw cycles.
其他
Aviva Systems Biology总部位于加利福尼亚州圣迭戈，在中国北京设有办公室，专注于为研究需求提供多克隆和单克隆抗体、ELISA试剂盒、蛋白质和定制服务。Aviva Systems Biology生产了24,000种经过验证的多克隆抗体，并提供近20,000种ELISA试剂盒，定制实验室服务包括蛋白表达和纯化、抗体开发，以及ELISA的开发、验证和生产。Aviva Systems Biology为与独特物种和靶标相关的研究提供独特工具，研究领域包括转录因子、癌症、心血管、细胞生物学、DNA损伤和修复、表观遗传学、信号转导、细胞分化、干细胞生物学等等。
