Anti-HSP90 beta Purified

Anti-HSP90 beta Purified

• Background: Hsp90 beta (heat shock protein 90 beta) is a constitutively expressed isoform of Hsp90, one of the most abundant chaperones in the cytosol of eukaryotic cells. Hsp90 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.
• Specifications: The antibody MBH90B recognizes the EEVHHG epitope within the N-terminal part of Hsp90 beta an ubiquitously expressed intracellular protein with calculated Mw of 83.3 kDa, however, migrating as a 90 kDa band under reducing SDS-PAGE conditions.
• CAS Number: 9007-83-4
• Certification: RUO
• Host: Mouse
• Species Reactivity: Cow, Human, Mouse
• Immunogen: Peptide corresponding to the EEVHHGEEEVEC sequence within N-terminal part of human Hsp90.
• Target Antigen: HSP90 beta
• Isotype: IgG1
• Clone: MBH90B
• Applications: Western blotting: Recommended dilution: 1 μg/mL. Immunocytochemistry: Recommended dilution: 1 μg/mL. Immunoprecipitation: Recommended dilution: 1 μg/mL.
• Validated Applications: IP, WB, ICC
• Concentration: 1 mg/mL
• Format: Purified
• Buffer: Stabilizing phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide
• References & Citations: *Kakeda M, Arock M, Schlapbach C, Yawalkar N: Increased expression of heat shock protein 90 in keratinocytes and mast cells in patients with psoriasis. J Am Acad Dermatol. 2014 Apr70(4):683-690., URL: https://pubmed.ncbi.nlm.nih.gov/24521827/,
• Other References: *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: http://www.ncbi.nlm.nih.gov/pubmed/9751071?ordinal,*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: http://www.ncbi.nlm.nih.gov/pubmed/15558465?ordina,*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: http://www.ncbi.nlm.nih.gov/pubmed/17681020?ordina,*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: http://www.ncbi.nlm.nih.gov/pubmed/18290764?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: http://www.ncbi.nlm.nih.gov/pubmed/9521088?ordinal,
• Storage Conditions: Store at 2-8°C. Do not freeze.