protein

HSPBP1 Protein, Human

HY-P701386

10 μg;50 μg

135;375 USD

HSPBP1 Protein, Human

proteins

E. coli

10 μg;50 μg

135;375 USD

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 is the recombinant human-derived HSPBP1 protein, expressed by E. coli , with tag free. The total length of HSPBP1 Protein, Human is 276 a.a., .

Human

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.

HSPBP1; Hsp70-binding protein 1; HspBP1; Heat shock protein-binding protein 1; Hsp70-binding protein 2; HspBP2; Hsp70-interacting protein 1; Hsp70-interacting protein 2

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

Supplied as a 0.22 μm filtered solution of 50 mM Tris-HCl, pH7.5, 200 mM NaCl, 20% glycerol.

Shipping with dry ice