HSP90AB1 Monoclonal Antibody
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Description
Overview of HSP90AB1 Monoclonal Antibody
HSP90AB1 Monoclonal Antibody is a highly specific reagent designed to detect and study the heat shock protein 90 alpha family class B member 1 (HSP90AB1), a molecular chaperone critical for protein folding, stability, and cellular stress responses. This antibody is widely used in research to investigate HSP90AB1’s role in cancer, viral infections, and cellular homeostasis. Below is a detailed analysis of its characteristics, applications, and research findings.
Clonal Diversity and Specificity
Multiple clones targeting HSP90AB1 have been developed, each with distinct properties:
Note: Rabbit polyclonal antibodies (e.g., Proteintech) offer broader species reactivity compared to mouse monoclonals .
Western Blotting
HSP90AB1 antibodies are extensively used to detect protein expression levels in lysates. For example:
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Clone 5G4: Detects HSP90AB1 in Jurkat, HeLa, HEK293, and NIH/3T3 cells .
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Proteintech (11405-1-AP): Validated in 35 publications for WB, with observed bands at 83–90 kDa .
Immunohistochemistry (IHC)
Used to localize HSP90AB1 in tissue sections. Clone 5G4 successfully stains human kidney cancer and brain tissues .
Immunofluorescence (IF)
Reveals subcellular localization. Clone 5G4 highlights HSP90AB1 in the cytoplasm of HeLa cells .
Protein Interaction Studies
Proximity Ligation Assay (PLA) with anti-HSP90AB1 and anti-NFKB1 antibodies detects interactions in HeLa cells, confirming HSP90AB1’s role in nuclear factor κB (NF-κB) signaling .
Viral Infections
HSP90AB1 is critical for viral replication:
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TGEV (Transmissible Gastroenteritis Coronavirus): HSP90AB1 knockdown reduces viral replication by ~42% in mRNA levels and ~1 log TCID50 in titers .
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SARS-CoV-2: HSP90 inhibitors (e.g., VER-82576) block infection by disrupting HSP90AB1-RNA interactions .
Cancer Therapeutics
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Chemoresistance: HSP90AB1 overexpression confers resistance to cisplatin in ovarian cancer by stabilizing IGF1R .
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Leukemia: HSP90AB1 inhibition synergizes with CDK7 inhibitors to overcome BCR-ABL1-mediated resistance in chronic myeloid leukemia .
Mechanistic Insights
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HSP90 Isoforms: HSP90AB1 (but not HSP90AA1) is essential for TGEV infection, highlighting isoform-specific roles .
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Proinflammatory Cytokines: HSP90AB1 knockdown reduces TGEV-induced IL-6, TNF-α, and CXCL10/CXCL11 expression .
Isoform Specificity
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HSP90AB1 and HSP90AA1 have distinct biological roles. Antibodies must avoid cross-reactivity (e.g., KW-2478 targets HSP90AA1 but not AB1) .
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Resistance Mechanisms: Prolonged HSP90 inhibitor use (e.g., PU-H71) can induce HSP90AB1 overexpression or mutations, reducing therapeutic efficacy .
Optimization Requirements
Product Specs
Buffer
Phosphate-buffered saline (PBS), pH 7.4, containing 0.02% sodium azide as a preservative and 50% glycerol.
Form
Liquid
Lead Time
Typically, we can ship products within 1-3 business days after receiving your order. Delivery time may vary depending on the purchasing method or location. Please consult your local distributors for specific delivery times.
Synonyms
90 kda heat shock protein beta HSP90 beta antibody; D6S182 antibody; FLJ26984 antibody; Heat shock 84 kDa antibody; Heat shock 90kD protein 1; beta antibody; Heat shock 90kDa protein 1 beta antibody; Heat shock protein 90 alpha family class B member 1 antibody; Heat shock protein 90 kDa antibody; Heat shock protein 90kDa alpha (cytosolic) class B member 1 antibody; Heat shock protein 90kDa alpha family class B member 1 antibody; Heat shock protein beta antibody; Heat shock protein HSP 90 beta antibody; Heat shock protein HSP 90-beta antibody; HS90B_HUMAN antibody; HSP 84 antibody; HSP 90 antibody; HSP 90 b antibody; HSP 90b antibody; HSP84 antibody; HSP90 BETA antibody; hsp90ab1 antibody; HSP90B antibody; HSPC2 antibody; HSPCB antibody
Target Names
Uniprot No.
Target Background
Function
HSP90AB1 is a molecular chaperone that plays a crucial role in the maturation, structural integrity, and proper regulation of specific target proteins involved in various cellular processes, including cell cycle control and signal transduction. It undergoes a functional cycle linked to its ATPase activity, which likely induces conformational changes in client proteins, leading to their activation. HSP90AB1 interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle, and chaperone function. These co-chaperones act as adapters, facilitating the interaction between HSP90AB1 and its client proteins. The recruitment of ATP and co-chaperones, followed by the binding of the client protein, forms a functional chaperone complex. Upon completion of the chaperoning process, the properly folded client protein and co-chaperone dissociate from HSP90AB1, leaving it in an ADP-bound, partially open conformation. Subsequently, ADP is released, and HSP90AB1 adopts an open conformation, ready for the next chaperoning cycle. Beyond its chaperone activity, HSP90AB1 also participates in the regulation of the transcription machinery. HSP90AB1 and its co-chaperones influence transcription at multiple levels. They can alter the steady-state levels of certain transcription factors in response to various physiological cues. Additionally, they modulate the activity of epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, to adapt to changes in the cellular environment. Furthermore, HSP90AB1 participates in the eviction of histones from the promoter region of specific genes, thereby activating gene expression. HSP90AB1 antagonizes STUB1-mediated inhibition of TGF-beta signaling by inhibiting STUB1-mediated SMAD3 ubiquitination and degradation. It promotes cell differentiation by chaperoning BIRC2, thereby protecting it from auto-ubiquitination and degradation by the proteasomal machinery. As a major chaperone, HSP90AB1 is involved in the phosphorylation and activation of STAT1 by chaperoning both JAK2 and PRKCE under heat shock conditions, ultimately activating its own transcription. HSP90AB1 also participates in the translocation of leaderless cargos, such as interleukin 1/IL-1, into the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). This translocation process is mediated by the cargo receptor TMED10.
Gene References Into Functions
- The production of IFN-gamma by T cells stimulated with citrullinated HSP90beta demonstrates a bias toward TH1 immune responses that are likely involved in the pathogenesis of rheumatoid arthritis-interstitial lung disease. PMID: 29968330
- The expression levels of HSP90AB1 can predict prognosis in astrocytic tumors. PMID: 27258564
- We found that the nutrient value of the culturing medium and the length of induction had a significant effect on Hsp90 production in Escherichia coli. Our fast, single-day purification protocol resulted in a stable, well-folded and pure sample that was resistant to degradation in a reproducible manner. PMID: 28651008
- Data show that the C allele of rs2282151 was associated with an increased expression level of heat shock protein 90 alpha family class B member 1 (HSP90AB1). PMID: 27756247
- Hsp90beta induced endothelial cell-dependent tumor angiogenesis by activating VEGFRs transcription. PMID: 28359326
- The authors find that the interaction between sB-Raf and the Hsp90 chaperone system is based on contacts with the M domain of Hsp90, which contributes to forming the ternary complex with Cdc37 as long as the kinase is not stabilized by nucleotide. PMID: 27620500
- High HSP90B expression is associated with laryngeal carcinoma. PMID: 27959448
- The expression level of Hsp90AB1 in lung cancer tissues was significantly higher than that in normal lung tissue and was associated with lung cancer pathological type and overall survival in lung adenocarcinoma patients. PMID: 26903158
- Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes. PMID: 26511315
- HSP90AB1: Helping the good and the bad PMID: 26358502
- These results suggest a means by which the hsp90beta interaction could prevent apo-sGCbeta1 from associating with its partner sGCalpha1 subunit while enabling structural changes to assist heme insertion into the H-NOX domain. PMID: 26134567
- Casein kinase 2-mediated phosphorylation of Hsp90beta and stabilization of PXR is a key mechanism in the regulation of MDR1 expression. PMID: 25995454
- This study identifies overexpression of HSP90 (especially isoform HSP90AB1) and its clients ATR, ATM, and NBS1 as promising markers for radioresistant, aggressive soft tissue sarcomas with particularly poor prognosis. PMID: 26044951
- The proteins (HSP90b, TMS1 and L-plastin) in the current study may hold potential in differentiating between melanoma and benign nevi in diagnostically challenging cases. PMID: 25191796
- The expression levels of Hsp90-beta and annexin A1 positively correlated and such co-overexpression of Hsp90-beta and annexin A1 contributed to lung cancer diagnosis. PMID: 25300907
- Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells. PMID: 24466266
- A novel mechanism for human carcinogenesis via methylation of HSP90AB1 by SMYD2. PMID: 24880080
- Hsp90 is upregulated in systemic sclerosis (SSc) and is critical for TGF-beta signalling. PMID: 23661493
- HSP70 was massively up-regulated in all mast cells three months after irradiation whereas HSP90AB1 was up-regulated only in a portion of mast cells PMID: 24670792
- Study obtained a structural model of Hsp90 in complex with its natural disease-associated substrate, the intrinsically disordered Tau protein. Hsp90 binds to a broad region in Tau that includes the aggregation-prone repeats. PMID: 24581495
- HSP90beta may positively regulate angiogenesis, not only as a protein chaperone, but also as an mRNA stabilizer for pro-angiogenic genes, such as BAZF, in a PRKD2 activity-dependent manner. PMID: 23515950
- Here we describe the specific association of heat shock protein-90-beta (Hsp90beta) with EV71 viral particles by the co-purification with virions using sucrose density gradient ultracentrifugation and colocalization as shown by immunogold EM. PMID: 23711381
- differences in expression caused by the -144 polymorphism in the HSP90beta promoter are associated with cellular inflammatory responses and the severity of organ injury PMID: 23516526
- the transdominant effect of HSP90AB1 on capsid-spacer protein 1-mutant HIV infectivity suggests a potential role for this class of cellular chaperones in HIV core stability and uncoating. PMID: 23200770
- The upregulation of Hsp90-beta was associated with poor post-surgical survival time and lymphatic metastasis of lung cancer patients PMID: 22929401
- DNA sequencing of 101 human samples detects eight and seven unique single nucleotide polymorphisms (SNPs) at the HSP90AA1 and HSP90AB1 loci, respectively. PMID: 22185817
- a possible role for HSP90AB1 in postentry HIV replication and may provide an attractive target for therapeutic intervention. PMID: 21602280
- TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. PMID: 21689689
- cyclophilin A and Hsp90 facilitate translocation of lethal factor(N) diphtheria toxin, but not of lethal factor, across endosomal membranes, and thus they function selectively in promoting translocation of certain proteins, but not of others PMID: 20946244
- Results show that RPL4, RPLP0, and HSPCB were the most stable reference genes in ovarian tissues. PMID: 20705598
- H. pylori induces the translocation of HSP90beta from the cytosol to the membrane and interaction of HSP90beta and Rac1, which leads to the activation of NADPH oxidase and production of ROS in gastric epithelial cells. PMID: 20451655
- findings present novel Hsp90 mutants that render cells resistant to Hsp90 inhibitors; show that the resistance depends on the increased ATPase turnover due to enhanced interaction with Aha1 PMID: 20226818
- Data show that the small molecule celastrol inhibits the Hsp90 chaperoning machinery by inactivating the co-chaperone p23, resulting in a more selective destabilization of steroid receptors. PMID: 19996313
- Study points to a potential role for Hsp90beta in MSC biology. PMID: 19327008
- PKC-epsilon is specifically required in the signaling pathway leading to the induction of hsp90 beta gene in response to heat shock. PMID: 14532285
- hsp90beta is repressed by p53 in UV irradiation-induced apoptosis PMID: 15284248
- Mutations at the phosphorylation sites of HSP90-beta modulate the interaction with arylhydrocarbon receptor (AhR) and may negatively regulate formation of the functional AhR complex in the steady-state cytosol. PMID: 15581363
- Hydrogen-exchange mass spectrometry was used to study structural & conformational changes undergone by full-length Hsp90beta in solution upon binding of the co-chaperone Cdc37 & 2 Hsp90 ATPase inhibitors: Radicicol & the anticancer drug DMAG PMID: 17764690
- Results suggest that HSP90 beta prevents auto-ubiquitination and degradation of its client protein c-IAP1, whose depletion would be sufficient to inhibit cell differentiation. PMID: 18239673
- These data provide an explanation for apoptosome inhibition by activated leukemogenic tyrosine kinases and suggest that alterations in Hsp90beta-apoptosome interactions may contribute to chemoresistance in leukemias. PMID: 18591256
- Presence of ovarian autoantibodies to human HSP90 in sera of women with infertility could be involved in human ovarian autoimmunity and thereby be a causative factor in early ovarian failure. PMID: 19022436
- Results show that heat shock protein 90 beta is cleaved by activated caspase-10 under UVB irradiation. PMID: 19380486
- celastrol may represent a new class of Hsp90 inhibitor by modifying Hsp90 C terminus to allosterically regulate its chaperone activity and disrupt Hsp90-Cdc37 complex. PMID: 19858214
Database Links
Protein Families
Heat shock protein 90 family
Subcellular Location
Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane. Dynein axonemal particle.
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