HSPH1 Antibody

Heat Shock Protein 105 (HSP105) is a member of the heat shock protein family, which plays a crucial role in cellular stress responses. HSP105 is also known as HSPH1 and is involved in various cellular processes, including protein folding, prevention of protein aggregation, and regulation of apoptosis.

HSP105 exists in two isoforms: HSP105α and HSP105β. HSP105α is constitutively expressed in the cytoplasm and functions as a molecular chaperone and apoptotic regulator. On the other hand, HSP105β is specifically expressed in the nucleus under stressed conditions and induces the expression of HSP70 through the activation of Stat3 .

HSP105 acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B. It promotes the release of ADP from HSPA1A/B, thereby triggering the release of client/substrate proteins. This mechanism is crucial for preventing the aggregation of denatured proteins in cells under severe stress, where ATP levels decrease markedly .

HSP105 has been implicated in various diseases, including cancer and neurodegenerative disorders. Its role as a molecular chaperone makes it a potential target for therapeutic interventions aimed at modulating protein folding and aggregation processes.

The Mouse Anti-Human HSP105 antibody is a monoclonal antibody specifically designed to target and bind to the HSP105 protein in human samples. This antibody is commonly used in research to study the expression and function of HSP105 in various cellular and disease contexts .

The Mouse Anti-Human HSP105 antibody is utilized in various applications, including:

• Western Blotting: To detect HSP105 protein levels in cell and tissue lysates.
• Immunohistochemistry: To visualize HSP105 expression in tissue sections.
• Flow Cytometry: To analyze HSP105 expression in cell populations.
• Immunoprecipitation: To isolate HSP105 protein complexes for further analysis.