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antibody from antibodies-online
Targeting: HSP90AA1
FLJ31884, Hsp89, Hsp90, HSP90N, HSPC1, HSPCA
Western blot
ImmunoprecipitationAntibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations
- Western blot [1]
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- Product number
- ABIN614807 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1) (N-Term) antibody
- Antibody type
- Monoclonal
- Description
- Protein-A affinity chromatography
- Reactivity
- Human, Mouse, Bovine
- Host
- Mouse
- Antigen sequence
EEVHHGEEEV EC- Epitope
- N-Term
- Isotype
- IgG
- Antibody clone number
- MBH90AB
- Vial size
- 0.1 mg
- Storage
- Store at 2 - 8°C for up to one month or (in aliquots) at -20°C for longer.
- Handling
- Avoid repeated freezing and thawing.
Submitted references The Hsp90 molecular chaperone: an open and shut case for treatment.
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.
Blind cavefish and heat shock protein chaperones: a novel role for hsp90alpha in lens apoptosis.
The Hsp90 complex--a super-chaperone machine as a novel drug target.
The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors.
Pearl LH, Prodromou C, Workman P
The Biochemical journal 2008 Mar 15;410(3):439-53
The Biochemical journal 2008 Mar 15;410(3):439-53
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.
Millson SH, Truman AW, Rácz A, Hu B, Panaretou B, Nuttall J, Mollapour M, Söti C, Piper PW
The FEBS journal 2007 Sep;274(17):4453-63
The FEBS journal 2007 Sep;274(17):4453-63
Blind cavefish and heat shock protein chaperones: a novel role for hsp90alpha in lens apoptosis.
Hooven TA, Yamamoto Y, Jeffery WR
The International journal of developmental biology 2004;48(8-9):731-8
The International journal of developmental biology 2004;48(8-9):731-8
The Hsp90 complex--a super-chaperone machine as a novel drug target.
Scheibel T, Buchner J
Biochemical pharmacology 1998 Sep 15;56(6):675-82
Biochemical pharmacology 1998 Sep 15;56(6):675-82
The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors.
Pratt WB
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.) 1998 Apr;217(4):420-34
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.) 1998 Apr;217(4):420-34
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