HSPBP1 Protein, Human

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., .

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

Tag Free

Q9NZL4 (R84-R359)

23640

30.9 kDa

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

Solution.

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

<1 EU/μg, determined by LAL method.

Please use rapid thawing with running water to thaw the protein.

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.