Hsp90 belongs to the heat shock protein family, which includes other members such as Hsp110, Hsp70, Hsp60, and small heat shock proteins. These family members share a distinctive C-terminal motif forATP binding. Hsp90 is one of the most abundant proteins in cells, with a molecular weight of approximately 90 kDa, and is essential for the viability of eukaryotes. Consequently, it is frequently used as a loading control in Western blotting. The Anti-Hsp90 Antibody-HRP is generated by conjugating Horseradish Peroxidase (HRP) to the Hsp90 antibody. During Western Blot detection, upon the addition of the chemiluminescent substrates A (typically Luminol) and B (Hydrogen Peroxide), HRP catalyzes the reaction between Luminol and Hydrogen Peroxide to form a peroxide. This peroxide is unstable and rapidly decomposes, yielding an excited-state intermediate. Fluorescence is emitted when this excited intermediate returns to its ground state, thereby enabling the detection of the Hsp90 loading control protein.