Product Details

Uniprot No.

P08238

Target Names

HSP90AB1

Alternative Names

Heat shock protein HSP 90-beta (HSP 90) (Heat shock 84 kDa) (HSP 84) (HSP84), HSP90AB1, HSP90B HSPC2 HSPCB

Species Reactivity

Human

Immunogen

A synthesized peptide derived from Human HSP90AB1

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

7F4

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Form

Liquid

Tested Applications

ELISA, IHC, FC

Recommended Dilution

Application	Recommended Dilution
IHC	1:50-1:200
FC	1:50-1:200

Protocols

ELISA Protocol
Immunohistochemistry (IHC) Protocol
Flow Cytometry (FC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Description

Generating a recombinant monoclonal antibody targeting HSP90AB1 involved several key steps. Initially, a rabbit was immunized with a synthesized peptide derived from human HSP90AB1 protein. B cells were subsequently isolated from the immunized rabbit, and RNA was extracted from these cells. The extracted RNA was reverse-transcribed into cDNA, which was utilized as a template to extend HSP90AB1 antibody genes using degenerate primers. These extended HSP90AB1 antibody genes were then integrated into a plasmid vector and introduced into host cells for expression. The HSP90AB1 recombinant monoclonal antibody was purified from the cell culture supernatant via affinity chromatography and evaluated for its suitability in ELISA, IHC, and FC assays, demonstrating specificity for human HSP90AB1 protein.

HSP90AB1 is a critical molecular chaperone that plays a central role in protein folding, stabilization, and regulation. Its diverse client protein repertoire includes key players in various cellular processes and signaling pathways. HSP90AB1's functions are essential for maintaining cellular homeostasis, adapting to stress, and supporting the proper functioning of numerous proteins with pivotal roles in health and disease.

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Target Background

Function

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 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. They first 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 involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the 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 expressions 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 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 C allele of rs2282151 was associated with 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 in 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

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Subcellular Location

Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane. Dynein axonemal particle.

Protein Families

Heat shock protein 90 family

Database Links

HGNC: 5258

OMIM: 140572

KEGG: hsa:3326

STRING: 9606.ENSP00000325875

UniGene: Hs.509736

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