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anti-Human HSP90 Anticorps:
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Chicken Monoclonal HSP90 Primary Antibody pour AA, ELISA - ABIN361717
Loo, Jensen, Cui, Hou, Chang, Riordan: Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. dans The EMBO journal 1999
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Human Polyclonal HSP90 Primary Antibody pour ICC, IF - ABIN361823
Arlander, Eapen, Vroman, McDonald, Toft, Karnitz: Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. dans The Journal of biological chemistry 2003
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Human Polyclonal HSP90 Primary Antibody pour IHC, ELISA - ABIN233817
Dedes, Dedes, Imesch, von Bueren, Fink, Fedier: Acquired vorinostat resistance shows partial cross-resistance to 'second-generation' HDAC inhibitors and correlates with loss of histone acetylation and apoptosis but not with altered HDAC and HAT activities. dans Anti-cancer drugs 2009
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Human Monoclonal HSP90 Primary Antibody pour ICC, IF - ABIN361731
Dalman, Bresnick, Patel, Perdew, Watson, Pratt: Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro. dans The Journal of biological chemistry 1989
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Fish Polyclonal HSP90 Primary Antibody pour WB - ABIN361873
Barent, Nair, Carr, Ruan, Rimerman, Fulton, Zhang, Smith: Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes. dans Molecular endocrinology (Baltimore, Md.) 1998
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Chicken Monoclonal HSP90 Primary Antibody pour IHC (p), IP - ABIN410090
Wang, Cheng, Chen, Chen, Tang, Chen, Lee, Huang: Changes in protein expression in testes of L2 strain Taiwan country chickens in response to acute heat stress. dans Theriogenology 2014
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Human Monoclonal HSP90 Primary Antibody pour WB - ABIN3043076
Jiang, Wang, Li, Shi, Li, Ma, Li, Luo, Yang, Xu: Heat shock protein 90-mediated inactivation of nuclear factor-?B switches autophagy to apoptosis through becn1 transcriptional inhibition in selenite-induced NB4 cells. dans Molecular biology of the cell 2011
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Bacteria Monoclonal HSP90 Primary Antibody pour FACS, IHC - ABIN151472
Kelly, Geoghegan, Feldman, Jain, Kauke, Le, Zhao, Wittrup: Chaperone proteins as single component reagents to assess antibody nonspecificity. dans mAbs 1970
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Human Monoclonal HSP90 Primary Antibody pour ICC, IF - ABIN361665
Minami, Kawasaki, Miyata, Suzuki, Yahara: Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90. dans The Journal of biological chemistry 1991
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Plasmodium falciparum Polyclonal HSP90 Primary Antibody pour ICC, IF - ABIN361683
Banumathy, Singh, Pavithra, Tatu: Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. dans The Journal of biological chemistry 2003
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Hsp90 protects cells from complement-dependent cytotoxicity by inhibiting, together with mortalin, C5b-9 assembly and/or stability at the plasma membrane.
Study reports that initial recruitment of co-chaperone Aha1 to Hsp90 is markedly enhanced by phosphorylation of a highly conserved tyrosine (Y313 in Hsp90alpha) in the Hsp90 middle domain Y313 represents a phosphorylation-sensitive conformational switch, engaged early after client loading, that affects both local and long-range conformational dynamics to facilitate initial recruitment of Aha1 to Hsp90.
correlation exists between USP22 and HSP90 expressions in gastric cancer and co-expression of USP22 and HSP90 may be more effective in predicting prognosis of gastric cancer
Fibroblasts isolated from pulmonary fibrosis lesions showed heightened Hsp90 ATPase activity compared with normal fibroblasts. The loss of the Hsp90AB, but not the Hsp90AA isoform, resulted in reduced fibroblast proliferation, myofibroblast transformation, and ECM production.
Objective measures of disease activity and inflammation in Crohn's disease were closely associated with HSP90alpha concentrations in plasma
the intracellular form of HSP90beta stabilises LRP1, thus amplifying HSP90alpha extracellular action
High Heat-shock protein-90 prolongs septic neutrophil survival by protecting c-Src kinase and caspase-8 from proteasomal degradation.
metazoan SIRT1 orthologs as Hsp90 clients and reveal a novel crosstalk between the proteostasis and nutrient signaling networks, which may have implications in various age related diseases.
This study evaluated the mechanism by which p23 triggers degradation of AHR, and the role of HSP90 in this process.
utilized homology modeling techniques to calculate full-length structures of human Hsp90alpha in closed and partially open conformations and used these structures as a basis for several molecular dynamics based analyses aimed at elucidating allosteric mechanisms and modulation sites in human Hsp90alpha
results of this integrative computational study are compared with a wide range of structural, biochemical, and cell-based experiments, offering a robust network-centric model of allosteric regulation and client kinase recognition by the Hsp90-Cdc37 chaperone machine
TOM34 and its partner HSP90AA1 might be used as a potential biomarker for monitoring HCV-induced hepatocellular carcinoma progression in the Egyptian population. Future large-scale validation studies are warranted.
RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex.
The study shows that a conserved tryptophan in the middle domain senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation-pi interaction with a neighboring lysine.
While activation in c-Src is strictly controlled by ATP-binding and phosphorylation, the authors find that activating conformational transitions are spontaneously sampled in Hsp90-dependent Src mutants.
chemotherapy agents can induce HSP90AA1 expression in osteosarcoma cells. And HSP90AA1, acting as an important regulator of autophagy, is a critical factor in the development of osteosarcoma chemoresistance both in vitro and in vivo. HSP90AA1 provides a novel therapeutic target for improving osteosarcoma treatment.
We confirm that miR-628-3p promotes apoptosis and inhibits migration in A549 cells by negatively regulating HSP90. Our results may reveal a novel strategy for lung cancer treatment
Data recognize HSP90 as a novel binding partner of PKM2 in hepatocellular carcinoma (HCC) cells. HSP90 potentiates the glycolysis and proliferation, reduces the apoptosis and thus enhances the growth of HCC cells through PKM2 Thr-328 phosphorylation maintaining its stability.
EGFR expression stratified most pronounced among HSP90low tumours, where the EGFRhigh phenotype was associated with longer survival
the SGT1-HSP90 complex contributes to the E3 ligase activity of the CUL4A complex that is necessary for CENP-A ubiquitylation and CENP-A deposition at the centromere.
DAF-21 Ienterd this protein as newentry study explores the role and contribution of MAP Kinase pathway and its regulator protein DAF-21 involvement in the immunity against opportunistic pathogen P. mirabilis infection
We demonstrate that while DAF-16/FOXO is dispensable, the age-dependent suppression of cilia phenotypes in IFT mutants requires cell-autonomous functions of the HSF1 heat shock factor and the Hsp90 chaperone
We found that HLH-1-dependent myogenic conversion specifically induced the expression of putative HLH-1-regulated chaperones in differentiating muscle cells. Moreover, disrupting the putative HLH-1-binding sites on ubiquitously expressed daf-21(Hsp90) and muscle-enriched hsp-12.2(sHsp) promoters abolished their myogenic-dependent expressio
The activity of protein phosphatase 5 towards native clients, such as glucocorticoid receptor, is modulated by the middle- and C-terminal domains of Hsp90.
The N Terminus of CeCdc37 Is Sufficient to Interact with CeHsp90.
Suppression of misfolding in muscle cells is achieved not only by enhanced expression of HSP90 in muscle cells but also by elevated expression of HSP90 (Daf-21) in intestine or neuronal cells. This cell-nonautonomous control of HSP90 expression relies upon transcriptional feedback between somatic tissues that is regulated by the FoxA transcription factor PHA-4.
Hsp90 (DAF-21) appears to participate in the maintenance of muscle structures as a transiently associated diffusible factor
DAF-21 indirectly regulates the meiotic prophase/metaphase transition during oocyte development by ensuring the normal function of WEE-1.3.
PA28 is likely to function in collaboration with Hsp90.
Hsp90 binds close to the transcriptional start site of around one-third of all Drosophila coding genes.
The zymogen pro-Dcp-1 was found to interact with Hsp83 and undergo proteasomal regulation in an Hsp83-dependent manner.
Escargot and Scratch regulate neural commitment by antagonizing Notch activity in Drosophila sensory organs
Nup358 facilitates JH-induced Met nuclear transport in a manner dependent on importin beta and Hsp83.
We show that while Hsp70 or Hsp83 expression under normal or stress conditions was not affected by AR feeding, Hsp27 levels were elevated in AR-fed wild-type control as well as heat-shocked larvae
The results revealed that the high-fat diet augmented the rate of lipid peroxidation and SOD and CAT activity and induced a higher expression of HSP83 and MPK2 mRNA.
Hsp83 facilitates methoprene-tolerant nuclear import to modulate juvenile hormone signaling.
Interaction of Spag with both Hsp70 and Hsp90 suggests a model whereby R2TP would accompany clients from Hsp70 to Hsp90 to facilitate their assembly into macromolecular complexes.
Our results reveal that Hsp83 plays a heretofore unappreciated role in promoting APC/C function during cell cycle exit and suggest a mechanism by which Hsp90 inhibition could promote genomic instability and carcinogenesis
Using computational and biochemical analyses, study find that Hsp90 maintains and optimizes RNA polymerase II pausing via stabilization of the negative elongation factor complex.
Data suggest that that an Sgt1/Hsp90-LKB1-AMPK pathway acts redundantly with a microtubule-induced polarity pathway to generate neuroblast cortical polarity, and the absence of neuroblast cortical polarity can produce neuroblast tumors.
Piwi functions in Hsp90-mediated suppression of phenotypic variation
A natural genetic variation in Hsp90 may mediate the evolution of canalized morphological traits even if it does not influence the expression of variation for uncanalized traits.
Hsp90 is required for Ago2 to receive the small interfering RNA (siRNA) duplex from the RNA-induced silencing complex-loading complex in RNA interference.
To determine the effect of Hsp90 on quantitative trait variability we deconstructed genetic, stochastic and environmental components of variation in traits of genetically matched flies, differing only by Hsp90 loss-of-function or wild-type alleles.
Up to 120-fold differences in penetrance among six highly related selection lines, selected for and against a deformed eye trait, did not translate into measurable differences in viability, lifespan or competitive fitness.
Hsp83 mutations can generate new variation by transposon-mediated 'canonical' mutagenesis
Hsp90 masks variation affecting target pathways and traits in populations independent of purely nongenetic sources of variation
heat shock inhibits eIF4F activity, and Hsp90 mRNA translation is sensitive to eIF4F inactivation
The results suggest that a multicomponent protein chaperone complex involving both Hsp90 and Hsp70 signals the cessation of heat shock protein synthesis, the restoration of normal translation, and likely the establishment of thermotolerance.
ZMYND10 is a novel co-chaperone that confers specificity for the FKBP8-HSP90 chaperone complex towards axonemal dynein clients required for cilia motility.
Study found that the chaperone-defective Hsp90alpha-Delta mutant mice showed similar wound closure rate as the wild-type Hsp90alpha mice and provides direct support for non-chaperone, extracellular Hsp90alpha as a potential driver for normal wound closure.
ATM is the primary kinase responsible for phosphorylation of Hsp90alpha after exposure ionizing radiation.
Fusion of human SGT1 (hSGT1) to NOD1 LRR significantly enhanced the solubility, and the fusion protein was stabilized by coexpression of mouse Hsp90alpha.
The major capsid protein of the mouse polyomavirus VP1 binds microtubules, HSP90, promotes their acetylation and blocks the host cell cycle.
Artificially maintaining Hsp90alpha or knocking down Aarsd1L expression interferes with the differentiation of C2C12 myotubes.
Immune-mediated destruction of ovarian follicles associated with the presence of HSP90 antibodies.
identify that Hsp90alpha at the transition neck region represents a signalling platform on which IRS-1 interacts with intracellular downstream signalling molecules involved in IGF-1 receptor signalling.
The study demonstrated that HSP90alpha plays an important role in the biogenesis of fetal PIWI-interacting RNAs (piRNA), which act against the transposon activities, in mouse male germ cells.
Data show that the heat shock protein 90 (HSP90) isoforms HSP90AA1 and HSP90AB1 are responsible for maintaining proper cellular levels of BMAL1 protein.
deficiency does not affect immunoglobulin gene hypermutation and class switch but causes enhanced MHC class II antigen presentation
study identified the essential role of Hsp90 in iNOS gene transactivation
Hsp90alpha may be required to maintain and to activate these regulators and/or to disassemble the synaptonemal complex that holds homologous chromosomes together
extracellular Hsp90alpha promotes angiogenesis in an MMP-2-dependent manner.
Hsp90-ovalbumin peptide complexes bind to scavenger receptor expressed by endothelial cells (SREC-I) on the surface of antigen presenting cells.
Endogenous HSP90 is essential for cross-presentation of both soluble and cell-associated antigens in dendritic cells.
KLF4 inhibition by antisense oligonucleotides markedly decreased the constitutive expression of HSP90 (HSP84 and HSP86).
Data show that inhibition of Hsp90 engages a p53-dependent pathway to apoptosis.
Following exposure to elevated temperatures, higher amounts of Hsp90alpha are inside the nucleus, but not within the nucleoli.
Hsp90/Sec22b promotes the unconventional secretion of IL-1beta through an autophagosomal carrier during Mycoplasma hyopneumoniae infection.
This study firstly found that host chaperone heat shock protein 90 (Hsp90) had a positive regulatory effect on the porcine circovirus type 2 infection cycle in vitro.
Feed intake remains low whereas respiratory frequency and body temperature remain higher and expression of HSP90, CAT1, SGLT1 and GLUT4 increases in some tissues in pigs under chronic heat stress conditions.
HSP90AA1 sperm content and the prediction of the boar ejaculate freezability.
Hsp90 is a modulator of eNOS activity and vascular reactivity in the newborn piglet pulmonary circulation
Apo-Hsp90 is in a conformational equilibrium between two open states that have never been described previously.
Findings indicate an essential role for Hsp90 in nongenomic estrogen signaling in coronary artery smooth muscle cells.
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.
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. Hspalpha may play a role in myogenesis.
The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene.
, epididymis luminal secretory protein 52
, heat shock 86 kDa
, heat shock 90kD protein 1, alpha
, heat shock 90kD protein 1, alpha-like 4
, heat shock 90kD protein, alpha-like 4
, heat shock 90kDa protein 1, alpha
, heat shock protein HSP 90-alpha
, renal carcinoma antigen NY-REN-38
, heat shock protein Hsp90
, heat shock protein 90
, Heat Shock Protein 90
, heat shock protein 83
, enhancer of sevenless 3A
, enhancer of seven in absentia 2
, heat shock protein 1, alpha
, heat shock protein 86
, heat shock protein 90kDa alpha (cytosolic), class A member 1
, heat shock protein, 1
, heat shock protein, 86 kDa 1
, heat shock protein, 89 kDa
, tumor-specific transplantation 86 kDa antigen
, 90-kDa heat shock protein
, Heat shock protein HSP 90-beta-like protein
, heat shock protein HSP 90-beta
, hsp90 alpha
, heat shock protein-90