Human HSP90 Antibody Summary
Accession # P08238
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Human HSP90 by Western Blot. Western blot shows lysates of Jurkat human acute T cell leukemia cell line, Raji human Burkitt's lymphoma cell line, HeLa human cervical epithelial carcinoma cell line, and SH-SY5Y human neuroblastoma cell line. PVDF membrane was probed with 0.5 µg/mL Goat Anti-Human HSP90 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3286) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). For additional reference, recombinant human HSP90a and HSP90 beta (5 ng/lane) were included. A specific band for HSP90 was detected at approximately 90 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.
Detection of Human HSP90 by Simple WesternTM. Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line and Raji human Burkitt's lymphoma cell line, loaded at 0.2 mg/mL. A specific band was detected for HSP90 at approximately 93 kDa (as indicated) using 5 µg/mL of Goat Anti-Human HSP90 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3286) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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 is to HSP90AB1-isoform 1, a 724 amino acid protein that is constitutively expressed. HSP90AB1-1 is also known as HSP90 beta, HSP90B, HSPCB, HSPC2, and HSP89 beta. The inducible form, HSP90AA1, is a 737 amino acid protein also known as HSP90 alpha, HSP90A, HSPC1, HSPCA, HSP89 alpha and LAP2. HSP90AB1‑1 and HSP90AA are 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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