The STIP1 Antibody from MyBioSource.com is a Rabbit Polyclonal antibody to STIP1. This antibody recognizes Human, Mouse, and Rat antigen. The STIP1 Antibody has been shown to work in the following applications: EIA, Immunoassay, ELISA, Immunohistochemistry, and Western Blot.
Description
HOP, also known as stress-induced phospho protein 1 (STIP), is a co-chaperone to the major heat shock proteins, Hsp70 and Hsp90, and appears in early receptor complexes (1, 2). Through mutual binding to both Hsp70 and Hsp90, Hop functions as an adaptor that can integrate Hsp70 and Hsp90 interactions (3, 4). HOP is an abundant and highly conserved protein which is composed of three tetratricopeptide repeat (TPR) domains (TPR1, TPR2a and TPR2b) and two DP repeat domains (DP1 and DP2), whose function has not been fully resolved (5).
Function: Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity).
Subunit Structure: Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Forms a complex with HSPA8/HSC70, HSPCA/HSP-86 and HSPCB/HSP-84 (By similarity). Interacts with PACRG (PubMed:14532270). Interacts with METTL21B (PubMed:23349634). Interacts with HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1 interaction (PubMed:9195923, PubMed:27353360). Interacts with FLCN, FNIP1 and FNIP2 (PubMed:27353360). Interacts with HSPA8/HSC70 (By similarity). Interacts with HSP90AB1; upon SMYD2-dependent HSP90AB1 methylation (PubMed:24880080).
Similarity: The TPR 1 repeat interacts with the C-terminal of HSC70. The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9 repeats (also called TPR2B domain) interact with HSP90