Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

抗体

TRAP1单克隆抗体(9B6)

ADI-SPA-971-0050

50微克

单克隆

小鼠

未共轭

9B6

人类, 小鼠

ADI-SPA-971-0050

TRAP1单克隆抗体(9B6)

小鼠

单克隆

抗体

50微克

9B6

IgG2a

人类, 小鼠

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. Recently TRAP1 has been identified as a protective element for cell survival, and has been suggested as a novel target for anti-cancer therapeutics.

HSP75, Mitochondrial HSP90, TNF receptor-associated protein 1, MtHSP90

重组人类TRAP1

液体。 在PBS, pH值7.2, 含50% 甘油和0.09% 叠氮化钠

Detects a band of ~72kDa by Western blot.

免疫印迹

-20°C