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|Tested species reactivity||Human, Mouse, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A synthetic phosphopeptide derived from human HSP90B around the phosphorylation site of Ser226 (E-I-SP-D-D)|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.4, with 150mM NaCl, 50% glycerol|
|Contains||0.02% sodium azide|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:500-1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1, an inducible form, and HSP90AB1, a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
heat shock 84 kDa; heat shock 90kD protein 1, beta; heat shock 90kDa protein 1, beta; heat shock protein 1, beta; heat shock protein 90 kDa; heat shock protein 90kDa alpha (cytosolic), class B member 1; heat shock protein 90kDa alpha family class B member 1; heat shock protein HSP 90-beta; heat shock protein, 84 kDa 1; HSP 84; HSP84; HSP90-beta; HSP90AB1; HSP90B; HSPC2; HSPCB; retinal degeneration slow protein; TSTA; tumor-specific transplantation 84 kDa antigen
90kDa; AL022974; C81438; D6S182; HSP84; Hsp84-1; Hsp90; HSP90-BETA; HSP90AB1; HSP90B; HSPC2; HSPCB