|Detection of Human HSP90 alpha by Western Blot. Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line. PVDF membrane was probed with 0.5 µg/mL of Rabbit Anti-Human HSP90 alpha Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7247) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). For additional reference, recombinant human HSP90 alpha and recombinant human HSP90 beta (5 ng/lane) were included. A specific band was detected for HSP90 alpha at approximately 90 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
The heat shock protein-90 kDa (HSP90) is a composite name for a large group of genes whose molecular weights average 90 kDa. HSP90 functions primarily as a molecular chaperone, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific degradative pathways. HSP90 is ubiquitously expressed, highly conserved and accounts for 1‑2% of the total cellular protein. Recently introduced, standardized nomenclature has divided the 17 identified HSP90 genes into three related and one unrelated classes, HSP90AA1, HSP90AB, HSP90BB, and TRAP, respectively. Six of these genes were functional while the remaining 11 are considered putative pseudogenes. Eukaryotic cells have two principal forms of HSP90. The AF7247 antibody described here is specific to HSP90 the inducible form, HSP90AA1, also known as HSP90 alpha, HSP90A, HSPC1, HSPCA and HSP86. The other form is a constitutively expressed HSP90AB1 that is a 724 amino acid protein that is also known as HSP90-beta, HSP90B, HSPCB, HSPC2, and HSP89-beta. HSP90AB1-1 and HSP90AA share 90% identity. In addition to its role as a molecular chaperone and stress response protein, HSP90 is a central component in a number of basic cellular processes including hormone signaling and cell cycle control.
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