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HSP90 beta (HSP90AB1) antibody RabMAb®

Cat.#: 1492-1

Rabbit Monoclonal Antibody


Clone ID: E296
Swiss Prot: P08238
Mol Weight: 92kDa
Size: 100ul
Price: $260
Availability: Ship next business day
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Description

The 90-kDa heat shock protein (Hsp90) is a highly conserved, and abundant cytosolic homodimeric molecular chaperone (1). Hsp90 is distinguished from other chaperones in that most of its known substrates are signal transduction proteins, non activated steroid hormone receptors, several protooncogenic tyrosine and serine/threonine kinases and actin (2-3). Two isoforms which correspond to the major and minor isoform , (Hsp90 α and Hsp90 β ) can be found in nearly equal amount in humans, and operates as part of a multichaperone machinery in the cytosol, which includes Hsp70, peptidyl-prolyl isomerases and other cochaperones (3).

Recommended Applications

WB, IHC, ICC, IP, FC

Applications and Recommended Dilution Factors

WB: 1:500
IHC: 1:50
ICC: 1:50
IP: 1:40
FC: 1:10

Species Reactivity *

Human, Mouse, Rat

*Cross reactivity determined by western blot only.


Products Data

A. Western blot analysis on Hela cell lysate using anti-Hsp90 Beta (N-term) RabMAb (catalog #1492-1).B. Immunohistochemical analysis of paraffin-embedded urinary bladder carcinoma tissue using anti-Hsp90 Beta (N-term) RabMAb (catalog #1492-1).

Specificity

A synthetic peptide corresponding to residues in N-terminus of human Hsp90 β was used as immunogen.

Storage Condition and Buffer

Store at -20 °C. Buffer: Antibody buffer, sodium azide, glycerol, and BSA. Stable for 12 months from date of receipt.

Alternative Names

HSP90AB1 antibody, D6S182 antibody, FLJ26984 antibody, HSP90-BETA antibody, HSP90B antibody, HSPC2 antibody, HSPCB antibody, Heat shock protein HSP 90-beta antibody, Heat shock 84 kDa antibody

Description References

1. Lees-Miller S., Anderson C.W.; Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II.;J. Biol. Chem. 264:2431-2437(1989).
2. Lees-Miller S., Anderson C.W.; The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues.; J. Biol. Chem. 264:17275-17280(1989).
3. Lotz G.P., Lin H., Harst A., Obermann W.M.J.; Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.; J. Biol. Chem. 278:17228-17235(2003).

Product References

1. Ge F, Lu XP, Zeng HL, et al, Proteomic and Functional Analyses Reveal a Dual Molecular Mechanism Underlying Arsenic-Induced Apoptosis in Human Multiple Myeloma Cells ,J. Proteome Res. 8 (2009) 3006–3019
[Application: WB]

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