Cell Signaling Technology

Product Pathways - Protein Folding

Phospho-HSP90α (Thr5/7) Antibody #3488

No. Size Price
3488S 100 µl ( 10 western blots ) ¥3,900.00 现货查询 购买询价
3488 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat,Monkey, Endogenous 90 Rabbit

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,

Specificity / Sensitivity

Phospho-HSP90α (Thr5/7) Antibody detects endogenous levels of HSP90α only when phosphorylated at Thr5/7.

Phospho-HSP90α (Thr5/7) Antibody识别内源性的Thr5/7磷酸化的HSP90α蛋白。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr5/7 of human HSP90α. Antibodies are purified by protein A and peptide affinity chromatography.


Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa and COS cells, treated with either λ phosphatase or UV, using Phospho-HSP90α (Thr5/7) Antibody and β-Actin Antibody #4967 as a loading control.

对HeLa和COS细胞,进行λ磷酸酶或紫外线处理,使用Phospho-HSP90α (Thr5/7) Antibody和β-Actin Antibody #4967作为上样对照进行Western blot分析。


HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP and co-chaperone dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).


Phospho-HSP90α (Thr5/7) Antibody is directed against the HSP90α threonine phosphorylation site at Thr5/7 that was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's MS/MS platform for phosphorylation site discovery. Phosphorylation of HSP90α at Thr5/7 was previously observed by the human double-stranded DNA-activated protein kinase (5). Please visit PhosphoSitePlus®, CST's modification site knowledgebase, at www.phosphosite.org for more information.

Phospho-HSP90α (Thr5/7) Antibody直接针对HSP90α在Thr5/7位点磷酸化的蛋白,该位点由由CST公司使用PhosphoScan发现,其是CST的基于质谱的磷酸化位点发现平台。以往研究也发现HSP90α在Thr5/7的磷酸化是由人双链DNA活化的蛋白激酶导致的(5)。请参见PhosphoSitePlus®,CST修饰位点知识库,www.phosphosite.org。

  1. Nollen, E.A. and Morimoto, R.I. (2002) J. Cell Sci. 115, 2809-2816.
  2. Young, J.C. et al. (2003) Trends Biochem. Sci. 28, 541-547.
  3. Pratt, W.B. and Toft, D.O. (2003) Exp. Biol. Med. 228, 111-133.
  4. Hohfeld, J. et al. (2001) EMBO Rep. 2, 885-890.
  5. Lees-Miller, S.P. and Anderson, C.W. (1989) J Biol Chem 264, 17275-80.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.

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