|Detection of Human/Mouse/Rat HSP90 by Western Blot. Western blot shows lysates of Jurkat human acute T cell leukemia cell line, A20 mouse B cell lymphoma cell line, and L6 rat myoblast cell line. PVDF membrane was probed with 0.5 µg/mL Human/Mouse/Rat HSP90 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3775) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). For additional reference, recombinant human HSP90a and HSP90b (5 ng/lane) were included. A specific band for HSP90 was detected at approximately 96 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
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, HSP90aa, HSP90AB, HSP90BB, and TRAP, respectively. Six of these genes were functional while the remaining 11 are considered putative pseudogenes. Eukaryotic cells have two principal isoforms of HSP90. The antibody described here was raised against the inducible form, HSP90AA1, a 732 amino acid protein also known as HSP90-alpha, HSP90A, HSPC1, HSPCA, HSP89-alpha and LAP2. The constitutively expressed HSP90AB1-isoform 1 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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