Human HSP90 alpha Antibody Summary
Asp702-Met716
Accession # P07900
Applications
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.
Scientific Data
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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 HSP90a Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7247) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). For additional reference, recombinant human HSP90a and recombinant human HSP90 beta (5 ng/lane) were included. A specific band was detected for HSP90a at approximately 90 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
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Western Blot Shows Human HSP90 alpha Specificity by Using Knockout Cell Line. Western blot shows lysates of HEK293T human embryonic kidney parental cell line and HSP90a knockout HEK293T cell line (KO). PVDF membrane was probed with 0.5 µg/mL of Rabbit Anti-Human HSP90a Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7247) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for HSP90a at approximately 96 kDa (as indicated) in the parental HEK293T cell line, but is not detectable in knockout HEK293T cell line. GAPDH (Catalog # AF5718) is shown as a loading control. This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
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.
Background: HSP90 alpha
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.
Product Datasheets
Citations for Human HSP90 alpha Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 2
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Heat Shock Proteins HSPA1 and HSP90AA1 Are Upregulated in Colorectal Polyps and Can Be Targeted in Cancer Cells by Anti-Inflammatory Oxicams with Arylpiperazine Pharmacophore and Benzoyl Moiety Substitutions at Thiazine Ring
Authors: I Szczuka, J Wierzbicki, P Serek, BM Szcz??niak, M Krzystek-K
Biomolecules, 2021-10-27;11(11):.
Species: Human
Sample Types: Cell Culture Supernates
Applications: Western Blot -
LRRC31 is induced by IL-13 and regulates kallikrein expression and barrier function in the esophageal epithelium
Authors: R J D'Mello, J M Caldwell, N P Azouz, T Wen, J D Sherrill, S P Hogan et al.
Mucosal Immunology
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