Stress-induced-phosphoprotein 1 (STI1) functions as a co-chaperone for HSP70 and HSP90 during heat shock response. STI1 exists as either a monomer or a dimer, and this conformational flexibility facilitates its function in organizing HSP70/HSP90. HSP90 acts as an ATPase, and requires the recruitment of client proteins and proper conformation to function. STI1 acts as a "scaffold" for client protein recruitment to the relaxed, ADP-bound conformation of HSP90, thus suppressing ATP turnover during the loading phase and allowing proper function.
Background References
1. Woodford M R et al. The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding. Nat Commun 7:12037-12037 (2016).
2. Silverstein A M et al. Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin. J Biol Chem 272:16224-16230 (1997).
Western blot analysis of STIP1 on different lysates with Rabbit anti-STIP1 antibody (ET7107-63) at 1/1,000 dilution.
Lane 1: Mouse testis tissue lysate Lane 2: Rat testis tissue lysate
Lysates/proteins at 20 µg/Lane. Exposure time: 5 minutes; ECL: K1801
Blocking: 5% NFDM/TBST, 1 hour at room temperature Primary antibody: ET7107-63, 1/1,000 in 5% NFDM/TBST, 2 hours at room temperature Secondary antibody: Goat anti-Rabbit IgG-HRP (HA1001), 1/100,000 in 5% NFDM/TBST, 1 hour at room temperature
Predicted band size: 63 kDa Observed band size: 63 kDa
Immunohistochemical analysis of paraffin-embedded human colon cancer tissue using anti-STIP1 antibody. Counter stained with hematoxylin.
Immunohistochemical analysis of paraffin-embedded human spleen tissue using anti-STIP1 antibody. Counter stained with hematoxylin.
Immunohistochemical analysis of paraffin-embedded mouse testis tissue using anti-STIP1 antibody. Counter stained with hematoxylin.
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