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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. in The Journal of biological chemistry 2003
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These findings identify the Ezh2 (show EZH2 Proteins)-Hsp90 (show HSP90 Proteins) 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 (show HSP90 Proteins) and the PI3K/AKT (show AKT1 Proteins)/mTOR (show FRAP1 Proteins) pathway in prostate cancer.
genes respond to HSP90 (show HSP90 Proteins) inhibition in a manner dependent on their genomic location with regard to strain-specific endogenous retroviruses-insertion sites.
PABPN1 (show PABPN1 Proteins) interacts with and is stabilized by heat shock protein 90 (show HSP90 Proteins).
Hyperacetylation of Hsp90 (show HSP90 Proteins) is a predictor and causal molecular determinant of stress resilience in mice. Brain-penetrant histone deacetylase 6 (show HDAC6 Proteins) inhibitors increase Hsp90 (show HSP90 Proteins) acetylation and modulate GR chaperone dynamics.
These findings demonstrate a critical role of Hsp90 (show HSP90 Proteins) in lipopolysaccharide (LPS (show TLR4 Proteins)) signaling, and a potential involvement of the heat shock response in LPS (show TLR4 Proteins)-induced preconditioning.
Phosphoproteomics, protein expression inference and signaling pathway prediction analysis of P2RX7 (show P2RX7 Proteins) signaling mediators pointed to HSPA2 (show HSPA2 Proteins) and HSP90 (show HSP90 Proteins) proteins.
Hsp90 (show HSP90 Proteins) inhibition plays a key role in preventing the recurrence of HCC (show FAM126A Proteins), and the combination of ablation with targeted therapy holds great potential to improve prognosis and survival of HCC (show FAM126A Proteins) patients.
These findings demonstrate CKII (show CSNK2A1 Proteins) induces polymerization of soluble TDP-43 (show TARDBP Proteins) into filaments and Hsp90 (show HSP90 Proteins) promotes TDP-43 (show TARDBP Proteins) filament depolymerization.
Data show that the heat shock protein 90 (HSP90 (show HSP90 Proteins)) isoforms HSP90AA1 (show HSP90AA1 Proteins) and HSP90AB1 are responsible for maintaining proper cellular levels of BMAL1 (show ARNTL Proteins) protein.
Data demonstrate that Hsp90alpha (show HSP90AA2 Proteins) and Hsp90beta exhibit similar interactions with co-chaperones, but significantly different behaviors with respect to substrate interactions under stress conditions.
We found that the nutrient value of the culturing medium and the length of induction had significant effect on Hsp90 (show HSP90 Proteins) 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 (show HSP90AA1 Proteins) 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 (show RAF1 Proteins) and the Hsp90 chaperone (show HSP90 Proteins) system is based on contacts with the M domain of Hsp90 (show HSP90 Proteins), which contributes in forming the ternary complex with Cdc37 (show CDC37 Proteins) 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 (show HSP90AA1 Proteins) 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 (show C9orf3 Proteins)-sGCbeta1 from associating with its partner sGCalpha1 subunit while enabling structural changes to assist heme insertion into the H-NOX domain.
Data from Xenopus laevis embryo suggest hsp90alpha (show HSP90AA2 Proteins) and hsp90Beta genes are conserved among vertebrates, and are differentially regulated in a tissue, stress, and development stage-specific manner.
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 (show TGFBR1 Proteins) and phosphorylated heat shock protein 27 specifically accumulate in the cytoskeleton fraction, and ALK1 (show ACVRL1 Proteins) and ALK5 (show TGFBR1 Proteins) interact with heat shock protein 90(HSP90 (show HSP90 Proteins)).
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
Mapped six genes (EIF4G3 (show EIF4G3 Proteins), HSP90, RBBP6 (show RBBP6 Proteins), IL8 (show IL8 Proteins), TERT (show TERT Proteins), 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 Protein 90, endoplasmic reticulum
, heat shock protein 90B
, heat shock protein hsp90 beta
, hsp90 beta
, HSP 84
, heat shock 84 kDa
, heat shock 90kDa protein 1, beta
, heat shock protein 90kDa alpha (cytosolic), class B member 1
, heat shock protein HSP 90-beta
, heat shock protein 1, beta
, heat shock protein, 84 kDa 1
, retinal degeneration slow protein
, tumor-specific transplantation 84 kDa antigen
, heat shock protein 90-beta
, heat shock protein 90kDa alpha, class B member 1
, heat shock cognate protein HSP 90-beta
, heat shock protein 90 beta
, heat shock 90kD protein 1, beta
, heat shock 90kDa protein beta
, Heat shock protein HSP 90-beta-like protein
, heat shock protein 90