Anti-HSP90 alpha/beta Purified

Anti-HSP90 alpha/beta Purified

• Background: Hsp90 (heat shock protein 90) is one of the most abundant chaperones in the cytosol of eukaryotic cells. It interacts with various proteins, including protein kinases and transcription factors, and either facilitates their stabilization and activation or directs them for proteasomal degradation. Hsp90 thus affects multiple signaling pathways and biological processes and modulation of this single target offers the prospect of simultaneous intervence to various key points of oncogenic transformation. Hsp90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis. There are two isoforms, alpha and beta, of vertebrate Hsp90. Whereas Hsp90 beta is expressed constitutively to a high level, Hsp90 alpha is stress-inducible and is overexpressed in many cancerous cells.
• Specifications: The antibody MBH90AB recognizes the epitope EEEVE within N-terminal part of ubiquitously expressed Hsp90 alpha and Hsp90 beta intracellular proteins with calculated Mw of 84.7 kDa and 83.3 kDa, respectively, however, migrating as 90 kDa bands under reducing SDS-PAGE conditions.
• CAS Number: 9007-83-4
• Certification: RUO
• Host: Mouse
• Species Reactivity: Cow, Mouse, Human
• Immunogen: Peptide corresponding to the sequence EEVHHGEEEVEC within N-terminal part of human Hsp90.
• Target Antigen: HSP90 alpha/beta
• Isotype: IgG1
• Clone: MBH90AB
• Applications: Western blotting: Recommended dilution: 1 μg/mL.
• Validated Applications: WB, IHC-P
• Concentration: 1 mg/mL
• Format: Purified
• Buffer: Stabilizing phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide
• References & Citations: *Reiter K, Aguilar PP, Wetter V, Steppert P, Tover A, Jungbauer A: Separation of virus-like particles and extracellular vesicles by flow-through and heparin affinity chromatography. J Chromatogr A. 2019 Mar 151588:77-84, URL: https://pubmed.ncbi.nlm.nih.gov/30616980/,
• Other References: *Millson SH, Truman AW, Rácz A, Hu B, Panaretou B, Nuttall J, Mollapour M, Söti C, Piper PW: Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicol. FEBS J. 2007 Sep274(17):4453-63., URL: https://www.ncbi.nlm.nih.gov/pubmed/17681020?ordin,*Pearl LH, Prodromou C, Workman P: The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J. 2008 Mar 15410(3):439-53., URL: https://www.ncbi.nlm.nih.gov/pubmed/18290764?ordin,*Hooven TA, Yamamoto Y, Jeffery WR: Blind cavefish and heat shock protein chaperones: a novel role for hsp90alpha in lens apoptosis. Int J Dev Biol. 200448(8-9):731-8., URL: https://www.ncbi.nlm.nih.gov/pubmed/15558465?ordin,*Scheibel T, Buchner J: The Hsp90 complex--a super-chaperone machine as a novel drug target. Biochem Pharmacol. 1998 Sep 1556(6):675-82., URL: https://www.ncbi.nlm.nih.gov/pubmed/9751071?ordina,*Pratt WB: The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med. 1998 Apr217(4):420-34., URL: https://www.ncbi.nlm.nih.gov/pubmed/9521088?ordina,
• Storage Conditions: Store at 2-8°C. Do not freeze.