Product Info

ELISA 1:10000, WB 1:500-1:2000, IHC 1:200-1:1000, IF/ICC 1:200-1:1000, FCM 1:200-1:400
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Monoclonal [AFB1899]
HSP90AB1 antibody detects endogenous levels of total HSP90AB1.
Cite Format: Affinity Biosciences Cat# BF0215, RRID:AB_2833923.
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


90 kda heat shock protein beta HSP90 beta; D6S182; FLJ26984; Heat shock 84 kDa; Heat shock 90kD protein 1, beta; Heat shock 90kDa protein 1 beta; Heat shock protein 90 alpha family class B member 1; 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 beta; Heat shock protein HSP 90 beta; Heat shock protein HSP 90-beta; HS90B_HUMAN; HSP 84; HSP 90; HSP 90 b; HSP 90b; HSP84; HSP90 BETA; hsp90ab1; HSP90B; HSPC2; HSPCB;



Purified recombinant fragment of human HSP90AB1 expressed in E. Coli.

Molecular chaperone. Has ATPase activity.

PTMs - P08238 As Substrate

Site PTM Type Enzyme
Y33 Phosphorylation
K36 Acetylation
K36 Ubiquitination
S45 Phosphorylation
S48 Phosphorylation
K53 Acetylation
K53 Ubiquitination
Y56 Phosphorylation
S58 Phosphorylation
T60 Phosphorylation
S63 Phosphorylation
K64 Acetylation
K64 Ubiquitination
S67 Phosphorylation
K69 Acetylation
K69 Ubiquitination
K72 Ubiquitination
T83 Phosphorylation
T85 Phosphorylation
T89 Phosphorylation Q6P2M8 (PNCK)
T94 Phosphorylation
K95 Ubiquitination
T104 Phosphorylation
K107 Ubiquitination
S108 Phosphorylation
K111 Ubiquitination
S124 Phosphorylation
K148 Ubiquitination
Y155 Phosphorylation
S159 Phosphorylation
S164 Phosphorylation
R177 Methylation
K180 Sumoylation
K180 Ubiquitination
K186 Acetylation
K186 Methylation
K186 Ubiquitination
T190 Phosphorylation
Y192 Phosphorylation
R196 Methylation
K204 Ubiquitination
S206 Phosphorylation
T214 Phosphorylation
Y216 Phosphorylation
K219 Acetylation
K219 Ubiquitination
S226 Phosphorylation P68400 (CSNK2A1)
K237 Ubiquitination
S255 Phosphorylation Q96GD4 (AURKB) , P68400 (CSNK2A1)
S261 Phosphorylation
K263 Acetylation
K273 Ubiquitination
K275 Acetylation
K275 Methylation
K275 Ubiquitination
Y276 Phosphorylation
K284 Acetylation
K284 Ubiquitination
T285 Phosphorylation
K286 Methylation
K286 Ubiquitination
T290 Phosphorylation
R291 Methylation
T297 Phosphorylation
Y301 Phosphorylation P12931 (SRC)
Y305 Phosphorylation
K306 Acetylation
K306 Sumoylation
K306 Ubiquitination
S307 Phosphorylation
T309 Phosphorylation
K319 Acetylation
K319 Ubiquitination
S322 Phosphorylation
K347 Acetylation
K347 Methylation
K347 Ubiquitination
K348 Acetylation
K348 Ubiquitination
K350 Ubiquitination
K354 Acetylation
K354 Ubiquitination
S365 Phosphorylation
S383 Phosphorylation
S391 Phosphorylation
S398 Phosphorylation
K399 Acetylation
K399 Sumoylation
K399 Ubiquitination
K402 Acetylation
K411 Ubiquitination
C412 S-Nitrosylation
K423 Acetylation
K423 Ubiquitination
K427 Acetylation
K428 Acetylation
K428 Ubiquitination
Y430 Phosphorylation
S434 Phosphorylation
K435 Acetylation
K435 Methylation
K435 Ubiquitination
K438 Ubiquitination
S445 Phosphorylation
T446 Phosphorylation
S452 Phosphorylation Q96GD4 (AURKB)
Y457 Phosphorylation
T459 Phosphorylation
S460 Phosphorylation
S462 Phosphorylation
T467 Phosphorylation
R475 Methylation
K477 Acetylation
K477 Ubiquitination
T479 Phosphorylation
K481 Acetylation
K481 Ubiquitination
S482 Phosphorylation
Y484 Phosphorylation
Y485 Phosphorylation
T487 Phosphorylation
S490 Phosphorylation
K491 Acetylation
K491 Ubiquitination
S497 Phosphorylation
K505 Ubiquitination
R506 Methylation
Y512 Phosphorylation
T514 Phosphorylation
Y520 Phosphorylation
K526 Acetylation
K526 Ubiquitination
K531 Acetylation
K531 Methylation
K531 Sumoylation
K531 Ubiquitination
S532 Phosphorylation
S535 Phosphorylation
T537 Phosphorylation
K538 Acetylation
K538 Ubiquitination
K550 Acetylation
K550 Ubiquitination
K551 Ubiquitination
K559 Acetylation
K559 Methylation
K559 Ubiquitination
C564 S-Nitrosylation
K565 Acetylation
K565 Methylation
K565 Ubiquitination
K568 Acetylation
K568 Ubiquitination
K573 Ubiquitination
K574 Acetylation
K574 Methylation
K574 Ubiquitination
K577 Ubiquitination
T579 Phosphorylation
S587 Phosphorylation
C589 S-Nitrosylation
C590 S-Nitrosylation
T593 Phosphorylation
S594 Phosphorylation
T595 Phosphorylation
Y596 Phosphorylation
T599 Phosphorylation
K607 Acetylation
K607 Methylation
K607 Ubiquitination
R612 Methylation
S615 Phosphorylation
T616 Phosphorylation
Y619 Phosphorylation
K623 Acetylation
K623 Methylation
K623 Ubiquitination
K624 Acetylation
K624 Ubiquitination
T637 Phosphorylation
R639 Methylation
K641 Ubiquitination
K649 Ubiquitination
S669 Phosphorylation
K685 Ubiquitination
S718 Phosphorylation Q9H4B4 (PLK3)

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. 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. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription.


Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).


S-nitrosylated; negatively regulates the ATPase activity.

Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction.

Methylated by SMYD2; facilitates dimerization and chaperone complex formation; promotes cancer cell proliferation.

Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation; disrupts the chaperoning function and the degradation of its client proteins.

Subcellular Location:

Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane.
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation (PubMed:18239673). Secreted when associated with TGFB1 processed form (LAP) (PubMed:20599762).

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

Monomer. Homodimer. Forms a complex with CDK6 and CDC37. Interacts with UNC45A; binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1 (By similarity). Interacts with DNAJC7. Interacts with FKBP4. May interact with NWD1. Interacts with SGTA. 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 STUB1 and SMAD3. Interacts with XPO1 and AHSA1. Interacts with BIRC2. Interacts with KCNQ4; promotes cell surface expression of KCNQ4. Interacts with BIRC2; prevents auto-ubiquitination and degradation of its client protein BIRC2. Interacts with NOS3. Interacts with AHR; interaction is inhibited by HSP90AB1 phosphorylation on Ser-226 and Ser-255. Interacts with STIP1 and CDC37; upon SMYD2-dependent methylation. Interacts with JAK2 and PRKCE; promotes functional activation in a heat shock-dependent manner. Interacts with HSP90AA1; interaction is constitutive. HSP90AB1-CDC37 chaperone complex interacts with inactive MAPK7 (via N-terminal half) in resting cells; the interaction is MAP2K5-independent and prevents from ubiquitination and proteasomal degradation. Interacts with CDC25A; prevents heat shock-mediated CDC25A degradation and contributes to cell cycle progression. Interacts with TP53 (via DNA binding domain); suppresses TP53 aggregation and prevents from irreversible thermal inactivation. Interacts with TGFB1 processed form (LAP); inhibits latent TGFB1 activation. Interacts with TRIM8; prevents nucleus translocation of phosphorylated STAT3 and HSP90AB1 (By similarity). Interacts with NR3C1 (via domain NR LBD) and NR1D1 (via domain NR LBD) (By similarity). Interacts with PDCL3 (By similarity). Interacts with TTC4 (via TPR repeats).


The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.

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). Hsp90β promotes aggressive vasculogenic mimicry via epithelial-mesenchymal transition in hepatocellular carcinoma. ONCOGENE, 2023 (PubMed: 30087438) [IF=8.0]

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). RETRACTED ARTICLE: Hsp90β promotes aggressive vasculogenic mimicry via epithelial–mesenchymal transition in hepatocellular carcinoma. Oncogene, 2018 (PubMed: 30087438) [IF=8.0]

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