HSPBP1 Protein, Human (E88G, His)

HSPBP1 protein regulates HSPA1A chaperone activity by inducing conformational changes in the ATP-binding domain and disrupting ATP binding. This interference inhibits the STUB1-mediated ubiquitination process and blocks chaperone-assisted degradation of immature CFTR. HSPBP1 Protein, Human (E88G, His) is the recombinant human-derived HSPBP1 protein, expressed by E. coli , with N-6*His labeled tag.

HSPBP1 Protein exerts regulatory control over HSPA1A chaperone activity by inducing conformational changes in the ATP-binding domain of HSPA1A, thereby disrupting ATP binding. This interference results in the inhibition of ubiquitination processes mediated by STUB1 and impedes the chaperone-assisted degradation of immature CFTR. The protein is known to interact with the ATP-binding domain of HSPA1A, forming a ternary complex with STUB1 and HSPBP1. Additionally, its interaction with PGLYRP1 serves to block the cytotoxic activity of the PGLYRP1-HSPA1A complex, highlighting the multifaceted regulatory roles of HSPBP1 in cellular processes.

Human

E. coli

N-6*His

Q9NZL4 (R84-R359, E88G)

23640

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.