Product: Hsp90 alpha Antibody
Catalog: AF5368
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Rabbit, Dog, Chicken
Mol.Wt.: 83 kD; 85kD(Calculated).
Uniprot: P07900
RRID: AB_2837853

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Pig(100%), Bovine(100%), Horse(100%), Rabbit(100%), Dog(100%), Chicken(100%)
Hsp90 alpha Antibody detects endogenous levels of total Hsp90 alpha.
Cite Format: Affinity Biosciences Cat# AF5368, RRID:AB_2837853.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


EL52; epididymis luminal secretory protein 52; Heat shock 86 kDa; heat shock 90kD protein 1, alpha; Heat shock 90kD protein 1, alpha like 4; heat shock 90kD protein, alpha-like 4; Heat shock 90kDa protein 1 alpha; Heat shock protein 90kDa alpha (cytosolic) class A member 1; Heat shock protein HSP 90-alpha; HS90A_HUMAN; HSP 86; HSP86; Hsp89; HSP89A; Hsp90; HSP90A; HSP90AA1; HSP90ALPHA; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; LAP 2; LAP2; lipopolysaccharide-associated protein 2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38;


FunctionMolecular chaperone. Has ATPase activity.Sequence similaritiesBelongs to the heat shock protein 90 family.Post-translational modificationsISGylated.



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P07900 As Substrate

Site PTM Type Enzyme
T5 Phosphorylation P78527 (PRKDC)
T7 Phosphorylation P78527 (PRKDC)
T36 Phosphorylation P68400 (CSNK2A1)
Y38 Phosphorylation P30291 (WEE1)
K41 Acetylation
K41 Ubiquitination
S52 Phosphorylation
S53 Phosphorylation
K58 Acetylation
K58 Ubiquitination
Y61 Phosphorylation
S63 Phosphorylation
T65 Phosphorylation
S68 Phosphorylation
K69 Acetylation
K69 Ubiquitination
S72 Phosphorylation
K74 Acetylation
K74 Sumoylation
K74 Ubiquitination
K84 Acetylation
K84 Ubiquitination
T88 Phosphorylation
T90 Phosphorylation P17612 (PRKACA)
T94 Phosphorylation
T99 Phosphorylation
K100 Acetylation
K100 Ubiquitination
T109 Phosphorylation
K112 Ubiquitination
S113 Phosphorylation
T115 Phosphorylation P05129 (PRKCG) , P33981 (TTK)
K116 Ubiquitination
K153 Ubiquitination
Y160 Phosphorylation
S164 Phosphorylation
S169 Phosphorylation
K185 Ubiquitination
K191 Acetylation
K191 Methylation
K191 Sumoylation
K191 Ubiquitination
T195 Phosphorylation
Y197 Phosphorylation
R201 Methylation
K204 Sumoylation
K204 Ubiquitination
K209 Ubiquitination
S211 Phosphorylation
Y216 Phosphorylation
T219 Phosphorylation
K224 Acetylation
K224 Ubiquitination
K228 Ubiquitination
S231 Phosphorylation P68400 (CSNK2A1)
K238 Ubiquitination
K245 Ubiquitination
S252 Phosphorylation
K255 Ubiquitination
S263 Phosphorylation P68400 (CSNK2A1)
K274 Acetylation
K276 Acetylation
K281 Ubiquitination
K283 Acetylation
K283 Methylation
K283 Ubiquitination
Y284 Phosphorylation
K292 Acetylation
K292 Ubiquitination
T293 Phosphorylation
K294 Acetylation
K294 Methylation
K294 Ubiquitination
R299 Methylation
T305 Phosphorylation
Y309 Phosphorylation
Y313 Phosphorylation
K314 Acetylation
K314 Sumoylation
K314 Ubiquitination
S315 Phosphorylation
T317 Phosphorylation
K327 Acetylation
K327 Ubiquitination
S330 Phosphorylation
R345 Methylation
R355 Methylation
K357 Sumoylation
K358 Sumoylation
K358 Ubiquitination
K362 Acetylation
K362 Ubiquitination
S391 Phosphorylation Q6P2M8 (PNCK)
S399 Phosphorylation
S406 Phosphorylation
K407 Acetylation
K407 Sumoylation
K407 Ubiquitination
K410 Acetylation
K419 Acetylation
K419 Ubiquitination
C420 S-Nitrosylation
T425 Phosphorylation P05129 (PRKCG)
K431 Acetylation
K431 Ubiquitination
Y434 Phosphorylation
K435 Acetylation
K436 Acetylation
K436 Ubiquitination
Y438 Phosphorylation
S442 Phosphorylation
K443 Acetylation
K443 Methylation
K443 Ubiquitination
K446 Ubiquitination
S453 Phosphorylation
K457 Ubiquitination
K458 Acetylation
K458 Ubiquitination
S460 Phosphorylation
R464 Methylation
Y465 Phosphorylation
Y466 Phosphorylation
T467 Phosphorylation
S468 Phosphorylation
S470 Phosphorylation
S476 Phosphorylation
K478 Acetylation
K478 Ubiquitination
C481 S-Nitrosylation
T482 Phosphorylation
K485 Acetylation
K485 Ubiquitination
K489 Acetylation
K489 Methylation
K489 Ubiquitination
Y492 Phosphorylation
Y493 Phosphorylation
T498 Phosphorylation
K499 Acetylation
K499 Ubiquitination
S505 Phosphorylation
R510 Methylation
K513 Acetylation
K513 Methylation
K513 Ubiquitination
Y528 Phosphorylation
K534 Acetylation
K539 Acetylation
K539 Sumoylation
K539 Ubiquitination
T540 Phosphorylation
S543 Phosphorylation
K546 Acetylation
K546 Ubiquitination
K558 Acetylation
K558 Ubiquitination
K559 Ubiquitination
K565 Ubiquitination
T566 Phosphorylation
K567 Acetylation
K567 Ubiquitination
K573 Acetylation
K573 Methylation
K573 Ubiquitination
K576 Acetylation
K576 Ubiquitination
K581 Acetylation
K581 Ubiquitination
K582 Ubiquitination
K585 Acetylation
K585 Ubiquitination
S589 Phosphorylation
S595 Phosphorylation
C597 S-Nitrosylation
C598 S-Nitrosylation
T601 Phosphorylation
S602 Phosphorylation
T603 Phosphorylation P05129 (PRKCG)
Y604 Phosphorylation
T607 Phosphorylation
K615 Acetylation
K615 Methylation
K615 Ubiquitination
S623 Phosphorylation
T624 Phosphorylation Q6P2M8 (PNCK)
Y627 Phosphorylation
K631 Acetylation
K631 Ubiquitination
K632 Acetylation
K632 Ubiquitination
S641 Phosphorylation
T645 Phosphorylation
K657 Ubiquitination
T669 Phosphorylation
Y689 Phosphorylation
T704 Phosphorylation
T708 Phosphorylation
S709 Phosphorylation
T725 Phosphorylation
S726 Phosphorylation

Research Backgrounds


Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation.



S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.

Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from the membrane and secretory pathways.

Subcellular Location:

Nucleus. Cytoplasm. Melanosome. Cell membrane.
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Homodimer. Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1. Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex. The closed form interacts (via the middle domain and TPR repeat-binding motif) with co-chaperone TSC1 (via C-terminus). Interacts with TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8. Interacts with KSR1. Interacts with co-chaperone CDC37 (via C-terminus); the interaction inhibits HSP90AA1 ATPase activity. May interact with NWD1. Interacts with FNIP1 and FNIP2; the interaction inhibits HSP90AA1 ATPase activity. Interacts with co-chaperone AHSA1 (phosphorylated on 'Tyr-223'); the interaction activates HSP90AA1 ATPase activity and results in the dissociation of TSC1 from HSP90AA1. Interacts with FLCN in the presence of FNIP1. Interacts with HSP70, STIP1 and PTGES3. Interacts with SMYD3; this interaction enhances SMYD3 histone-lysine N-methyltransferase. Interacts with SGTA (via TPR repeats). Interacts with TTC1 (via TPR repeats). Interacts with HSF1 in an ATP-dependent manner.. Interacts with MET; the interaction suppresses MET kinase activity. Interacts with ERBB2 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity. Interacts with HIF1A, KEAP1 and RHOBTB2. Interacts with HSF1; this interaction is decreased in a IER5-dependent manner, promoting HSF1 accumulation in the nucleus, homotrimerization and DNA-binding activities. Interacts with STUB1 and SMAD3. Interacts with HSP90AB1; interaction is constitutive. Interacts with HECTD1 (via N-terminus) (By similarity). Interacts with NR3C1 (via domain NR LBD) and NR1D1 (via domain NR LBD) (By similarity). Interacts with NLPR12. Interacts with PDCL3 (By similarity).

(Microbial infection) Interacts with herpes simplex virus 1 protein US11; this interaction inhibits TBK1-induced interferon production.


The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.

Belongs to the heat shock protein 90 family.

Research Fields

· Cellular Processes > Cell growth and death > Necroptosis.   (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.   (View pathway)

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Prostate cancer.   (View pathway)

· Organismal Systems > Immune system > Antigen processing and presentation.   (View pathway)

· Organismal Systems > Immune system > NOD-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > IL-17 signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Th17 cell differentiation.   (View pathway)

· Organismal Systems > Endocrine system > Progesterone-mediated oocyte maturation.

· Organismal Systems > Endocrine system > Estrogen signaling pathway.   (View pathway)


1). Meng J et al. Hsp90β promotes aggressive vasculogenic mimicry via epithelial-mesenchymal transition in hepatocellular carcinoma. Oncogene 2018 Aug 7 (PubMed: 30087438) [IF=7.971]

Application: IHC    Species: human    Sample: HCC cells

Fig. 1| Hsp90βassociates with vasculogenic mimicry and poor prog-nosis in HCC. e Representative images of Hsp90β, Hsp90α, VE-cadherin,E-cadherin, Vimentin, MMP2, and MMP9 expression in VM/Hsp90βnegative and positive HCC tissue samples. All images are repre-sentative.

Application: WB    Species: human    Sample: PLC-PRF-5 cells

Fig. 3| Hsp90β interacts with Twist1 in HCC. a Immunopurification and mass spectrometry analysis of Hsp90β-(left) and Twist1-associated proteins (right). b Whole-cell lysates from PLC-PRF-5 cells were immunoprecipitated (IP) followed by immunoblotting (IB)with antibodies against the indicated proteins.

2). Guan L et al. HSP90 Inhibitor Ganetespib (STA-9090) Inhibits Tumor Growth in c-Myc-Dependent Esophageal Squamous Cell Carcinoma. Onco Targets Ther 2020 Apr 8;13:2997-3011 (PubMed: 32308431) [IF=3.337]

Application: IF/ICC    Species: Human    Sample: Eca-109 cells

Figure 1 MYC was over-expressed and interacted with HSP90 in ESCC. (A and B) MYC’ nuclear expression in ESCC. Images from TMA immunostained for MYC. Scale bars represent 50 μm. (C) MYC expression against HSP90 expression status showing 50% of double-positive samples. (D) Western blotting examined the expression of MYC in ESCC tumor tissues and adjacent normal tissues (n=12). (E) Localization of HSP90 and MYC in Eca-109 cells by immunofluorescence. Scale bars represent 25 μm. (F) Interaction of endogenous HSP90 with MYC was detected by co-IP assays in Eca-109 cells. ***P < 0.001.

Application: WB    Species: Human    Sample: Eca-109 cells

Figure 1 MYC was over-expressed and interacted with HSP90 in ESCC. (A and B) MYC’ nuclear expression in ESCC. Images from TMA immunostained for MYC. Scale bars represent 50 μm. (C) MYC expression against HSP90 expression status showing 50% of double-positive samples. (D) Western blotting examined the expression of MYC in ESCC tumor tissues and adjacent normal tissues (n=12). (E) Localization of HSP90 and MYC in Eca-109 cells by immunofluorescence. Scale bars represent 25 μm. (F) Interaction of endogenous HSP90 with MYC was detected by co-IP assays in Eca-109 cells. ***P < 0.001.

3). Chen D et al. Comparative proteomics identify HSP90A, STIP1 and TAGLN‑2 in serum extracellular vesicles as potential circulating biomarkers for human adenomyosis. Exp Ther Med 2022 Jun;23(6):374. (PubMed: 35495589)

4). Comparative proteomics identify HSP90A, STIP1 and TAGLN‑2 in serum extracellular vesicles as potential circulating biomarkers for human adenomyosis.

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