Heat Shock Protein 90 beta, NT (HSP90b)

The 90kD 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 a and Hsp90 b ) 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).\n\nApplications: \nSuitable for use in Flow Cytometry, Western Blot, Immunoprecipitation, Immunohistochemistry, Immunocytochemistry. Other applications not tested.\n\nRecommended Dilution:\nFlow Cytometry: 1:10\nWestern Blot: 1:500\nImmunohistochemistry: 1:50\nImmunocytochemistry: 1:50\nImmunoprecipitation: 1:40\n\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot Freeze at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. \n\nManufactured incorporating RabMAb(R) technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.

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SPECIFICATIONS

Catalog Number

H1831-55C

Size

100ul

Applications

FC, ICC, IHC, IP, WB

Hosts

Rabbit

Reactivities

Hum, Mouse

Form

Supplied as a liquid.

P Type

Mab

Purity

Supernatant

Isotype

IgG

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).

Additional Info

Recognizes human Hsp90 beta.