What Is Recombinant Human HSPBP1 Protein?

Recombinant Human HSPBP1 Protein (SKU: rp368211) is a recombinantly produced form of the human Hsp70-binding protein 1. HSPBP1 is a cytosolic cochaperone that interacts directly with the nucleotide-binding domain of Hsp70 (HSPA family members), functioning as a nucleotide exchange factor inhibitor. By binding to Hsp70, HSPBP1 modulates the chaperone cycle, influencing protein folding, refolding of misfolded substrates, and cellular protein quality control. It is also reported to play roles in the inhibition of apoptosis through interactions with CHIP (C-terminus of Hsp70-interacting protein) and the regulation of ubiquitin-mediated protein degradation pathways.

Biological Function and Significance of HSPBP1

HSPBP1 belongs to the Hsp70 cochaperone network and acts primarily as a negative regulator of Hsp70-mediated protein folding. Its principal mechanism involves displacing ADP from the Hsp70 nucleotide-binding domain, which paradoxically slows the overall ATPase-driven folding cycle rather than accelerating it. This inhibitory regulation is physiologically important for fine-tuning proteostasis under both normal and stress conditions.

Research has implicated HSPBP1 in several disease-relevant processes: (1) it competes with CHIP for Hsp70 binding, thereby protecting certain client proteins from CHIP-mediated ubiquitination and proteasomal degradation; (2) it has been studied in the context of cancer cell survival, neurodegenerative disease models, and cardiac stress responses; and (3) it may influence the activity of Hsp90 client proteins indirectly through its effects on the Hsp70 system. These roles make HSPBP1 a relevant target for studies in proteostasis, stress biology, and drug discovery.

Product Specifications and Quality

Aladdin Scientific's Recombinant Human HSPBP1 Protein (rp368211) is produced using recombinant expression technology to ensure consistent lot-to-lot reproducibility and high purity suitable for demanding in vitro research applications. Researchers should consult the official product datasheet for confirmed details on expression system, tag configuration, molecular weight, purity grade, endotoxin levels, formulation buffer, and concentration, as these parameters are subject to lot-specific certificate-of-analysis values.

Typical quality attributes for recombinant proteins of this class include: SDS-PAGE-verified purity, biological activity confirmation via functional assay where applicable, and endotoxin testing. Please refer to the product page or contact Aladdin Scientific technical support for the most current and authoritative specifications for SKU rp368211.

Storage, Handling, and Stability

Proper storage and handling are critical to maintaining the activity and integrity of Recombinant Human HSPBP1 Protein. As a general guideline for recombinant proteins, the following practices are recommended until the official datasheet is consulted:

• Short-term storage: Store at 4°C if the protein will be used within 1–2 weeks of receipt.
• Long-term storage: Aliquot into single-use volumes and store at −20°C or −80°C to avoid repeated freeze-thaw cycles, which can cause protein aggregation and loss of activity.
• Handling: Thaw on ice and mix gently; avoid vortexing. Keep protein on ice during experimental setup.
• Carrier protein: If storing at low concentrations, consider adding a carrier protein such as BSA to prevent adsorption to container surfaces.

Always refer to the lot-specific datasheet supplied with the product for authoritative storage and stability information for rp368211.

Research Applications of HSPBP1

Recombinant Human HSPBP1 Protein is used across a range of in vitro and cell-free research applications that explore the Hsp70 chaperone network and cellular proteostasis:

• Biochemical interaction studies: Co-immunoprecipitation, pull-down assays, and surface plasmon resonance (SPR) to characterize HSPBP1 binding to Hsp70 or CHIP.
• ATPase inhibition assays: Measuring the effect of HSPBP1 on Hsp70 ATPase activity in reconstituted systems.
• Protein refolding assays: Assessing the impact of HSPBP1 on Hsp70-assisted refolding of model substrate proteins.
• Ubiquitination pathway studies: Investigating how HSPBP1 competition with CHIP modulates substrate ubiquitination and degradation.
• Drug discovery: Screening for small molecules that modulate the HSPBP1–Hsp70 interaction as a strategy to alter proteostasis in disease models.
• Apoptosis and stress biology: Examining HSPBP1's protective roles in cellular stress response models.