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Human HSP90AB1 Protein expressed in Baculovirus - ABIN1686667
Arlander, Eapen, Vroman, McDonald, Toft, Karnitz: Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. dans The Journal of biological chemistry 2003
Show all 10 Pubmed References
the intracellular form of HSP90beta stabilises LRP1, thus amplifying HSP90alpha extracellular action
the crosstalk between Hsp90ab1 and LRP5 contributed to the upregulation of multiple mesenchymal markers, which are also targets of Wnt/beta-catenin. Collectively, this study uncovers the details of the Hsp90ab1-LRP5 axis, providing novel insights into the role and mechanism of invasion and metastasis in gastric cancer (GC) .
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.
the expressions of HSP90AB1 can predict prognosis in astrocytic tumors
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.
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).
Hsp90beta induced endothelial cell-dependent tumor angiogenesis by activating VEGFRs transcription.
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.
High HSP90B expression is associated with laryngeal carcinoma.
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.
We revealed that Hsp90A and Hsp90B are partly colocalized with heparan sulfate proteoglycans (HSPGs) on the cell surface and that this colocalization was sensitive to heparin.
Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes.
HSP90AB1: Helping the good and the bad
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.
Casein kinase 2-mediated phosphorylation of Hsp90beta and stabilization of PXR is a key mechanism in the regulation of MDR1 expression.
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.
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.
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.
These results suggest that differences in the middle domain of Hsp90alpha and Hsp90beta may be responsible for the isoform-specific interactions with selected proteins.
CDC37 has an important role in chaperoning protein kinases; it stabilizes kinase clients by a mechanism that is not dependent on a substantial direct interaction between CDC37 and HSP90, but requires HSP90 activity
gene expression and promoter characterization
The results demonstrate that in renal cells, NHE1 is associated with several regulatory proteins including Hsp90, and that Hsp90 affects its function possibly through altered phosphorylation of the protein via the AKT kinase.
Extracellular Hsp70 and Hsp90, either in soluble form or secreted as part of exosomes from tumor cells, are responsible for tumor induction of cachexia.
a surface population of Hsp90 extracellularly binds TGFbetaRI and this complex behaves as an active participant in collagen production in TGFbeta-activated fibroblasts.
Hsp90 is highly expressed on the cell surface of melanoma cells, and synthetic agents that target Hsp90 are promising cancer therapeutic drugs
These findings identify the Ezh2-Hsp90 interaction as a previously unrecognized mechanism essential for T-cell responses and an effective target for controlling graft-versus-host disease.
Data show that docetaxel, rapamycin and tanespimycin multi-drug loaded micelles targeted against HSP90 and the PI3K/AKT/mTOR pathway in prostate cancer.
genes respond to HSP90 inhibition in a manner dependent on their genomic location with regard to strain-specific endogenous retroviruses-insertion sites.
PABPN1 interacts with and is stabilized by heat shock protein 90.
Hyperacetylation of Hsp90 is a predictor and causal molecular determinant of stress resilience in mice. Brain-penetrant histone deacetylase 6 inhibitors increase Hsp90 acetylation and modulate GR chaperone dynamics.
These findings demonstrate a critical role of Hsp90 in lipopolysaccharide (LPS) signaling, and a potential involvement of the heat shock response in LPS-induced preconditioning.
Phosphoproteomics, protein expression inference and signaling pathway prediction analysis of P2RX7 signaling mediators pointed to HSPA2 and HSP90 proteins.
Hsp90 inhibition plays a key role in preventing the recurrence of HCC, and the combination of ablation with targeted therapy holds great potential to improve prognosis and survival of HCC patients.
These findings demonstrate CKII induces polymerization of soluble TDP-43 into filaments and Hsp90 promotes TDP-43 filament depolymerization.
Data show that the heat shock protein 90 (HSP90) isoforms HSP90AA1 and HSP90AB1 are responsible for maintaining proper cellular levels of BMAL1 protein.
Reveal an opposite role of Hsp70 and Hsp90 in regulating TGF-beta signaling by implicating CHIP-mediated Smad3 ubiquitination and degradation. This study provides a new insight into understanding the regulation of the TGF-beta signaling by chaperones.
A novel role for Hsp90 in controlling PPARgamma stability and cellular differentiation, is reported.
inhibition exerts an anti-inflammatory effect in murine models of colitis
Hsp90 activity is necessary to control the expression, activity or location of specific kinases and motor proteins during the axon specification and axon elongation processes.
Alcohol-induced cilia stimulation occurs through the increased association of HSP90 with miR-122 target gene endothelial nitric oxide synthase (eNOS).
Results suggest that heat shock protein 90 inhibitor radicicol inhibited 3T3-L1 preadipocyte differentiation through affecting the PDK1/Akt pathway.
Data from Xenopus laevis embryo suggest hsp90alpha and hsp90Beta genes are conserved among vertebrates, and are differentially regulated in a tissue, stress, and development stage-specific manner.
Heat tolerance was assessed in Boran and Nguni cows. Protein levels of HSP90AB1, skin thickness, rectal and skin temperature were higher in the Boran cows than Nguni cows. Breed, age and coat colour did not influence HSP90AB1 concentration.
Studied the nucleotide polymorphism within the HSP90AB1 gene (SNP g.4338T>C) in Indian breeds of dairy cattle.
Association analysis revealed that the T allele at SNP g.4338T>C of the HSP90AB1 gene improved heat tolerance in cattle. Allele T was 100% in White Lamphun animals, 84% in Mountain cattle, and 18% in Holstein Friesian heifers.
This study showed that ubiquitinated ALK5 and phosphorylated heat shock protein 27 specifically accumulate in the cytoskeleton fraction, and ALK1 and ALK5 interact with heat shock protein 90(HSP90).
the protective effect exerted by HSP90 on eNOS degradation mediated by calpain represents a novel and critical mechanism that assures the reversibility of the intracellular trafficking and activation of the synthase
Data demonstrate that Hsp90alpha and Hsp90beta exhibit similar interactions with co-chaperones, but significantly different behaviors with respect to substrate interactions under stress conditions.
Mapped six genes (EIF4G3, HSP90, RBBP6, IL8, TERT, and TERC) on the chromosomes of Equus caballus, Equus asinus, Equus grevyi, and Equus burchelli by fluorescence in situ hybridization.
Hsp90 is involved in opposing signaling pathways of cartilage homeostasis and catabolic responses are more sensitive to Hsp90 inhibition than are anabolic responses.
This gene encodes a member of the heat shock protein 90 family\; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. This gene encodes the constitutive form of the cytosolic 90 kDa heat-shock protein and is thought to play a role in gastric apoptosis and inflammation. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes.
, heat shock 84 kDa
, heat shock 90kD protein 1, beta
, heat shock protein HSP 90-beta
, 94 kDa glucose-regulated protein
, heat shock protein 90 kDa beta member 1
, tumor rejection antigen (gp96) 1
, tumor rejection antigen 1
, Heat Shock Protein 90, endoplasmic reticulum
, heat shock protein 90B
, heat shock protein hsp90 beta
, hsp90 beta
, HSP 84
, heat shock 90kDa protein 1, beta
, heat shock protein 1, beta
, heat shock protein 90kDa alpha (cytosolic), class B member 1
, heat shock protein, 84 kDa 1
, retinal degeneration slow protein
, tumor-specific transplantation 84 kDa antigen
, heat shock cognate protein HSP 90-beta
, heat shock protein 90 beta
, heat shock 90kDa protein beta
, heat shock protein 90-beta
, heat shock protein 90kDa alpha, class B member 1
, Heat shock protein HSP 90-beta-like protein
, heat shock protein 90
, Heat shock protein HSP 90-beta