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Validated All-in-One™ qPCR Primer for HSP90AA1(NM_001017963.2) Search again
Product ID:
HQP009092
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
EL52, HEL-S-65p, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp103, Hsp89, Hsp90, LAP-2, LAP2
Gene Description:
heat shock protein 90 alpha family class A member 1
Target Gene Accession:
NM_001017963.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1, an inducible form, and HSP90AB1 (MIM 140572), a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM].
Gene References into function
- Cisplatin may provide a pharmacological tool to dissect C- and N-terminal nucleotide binding of Hsp90. A model is proposed on the interactions of the two nucleotide-binding domains and the charged region of Hsp90.
- These data indicate that sequences within the last one-fourth of hsp90 regulate ATP hydrolysis
- association of PDK1 with Hsp90 regulates its stability, solubility, and signaling
- Two distinct regions of the immunophilin-like protein XAP2 regulate dioxin receptor function and interaction with hsp90
- HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor
- we show that in mammals, the cytosolic chaperones Hsp90 and Hsp70 dock onto a specialized TPR domain in the import receptor Tom70 at the outer mitochondrial membrane.
- TPR2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
- Heat shock protein 90 is an endogenous protein enhancer of inducible nitric-oxide synthase
- nuclear localization of N-WASP modulates Src kinase activity by regulating HSP90 expression
- GRK2, GRK3, GRK5, and GRK6 are stabilized by interaction with Hsp90, revealing that GRK interaction with heat shock proteins plays an important role in regulating GRK maturation.
- HSP90 has a role in regulation of levels of Chk1 and sensitization of tumor cells to replication stress
- Hsp90, a molecular chaperone that is central to the cellular stress response, associates with survivin, an apoptosis inhibitor and essential regulator of mitosis.
- heteromeric complex containing the molecular chaperones Hsp90 and Cdc37/p50 interacts with the kinase domain of LKB1
- by induction of HSP90A c-Myc may control the activity of multiple signal pathways involved in cellular transformation
- Hsp90/p50cdc37 is required for mixed-lineage kinase (MLK) 3 signaling
- Hsp90 is expressed on the surface of tumor cells and is present in advanced malignant melanomas.
- In neurites, movement by diffusion is not possible, and we show that movement of the GFP-Glucocorticoid Receptor from neurites is blocked by geldanamycin, suggesting that the hsp90-dependent movement machinery is required for retrograde movement.
- the role of Hsp90 in nuclear retention of GR after ligand withdrawal
- the activation mechanism of HSP90 molecular chaperone that heat stress induces the liberation of the oligomerization/client-binding site of residues 311-350 by disrupting the intramolecular interaction between residues 289-389 and 401-546
- Hsp90 chaperone activity is important for the transcriptional activity of genotypically wild-type p53
- Hsp90 is required to maintain the folded, active state of p53 by a reversible interaction
- upregulation with ecNOS prevents apoptosis in endothelial cells induced by high glucose
- T cell immunity to Hsp70 and Hsp90, like Hsp60-specific immunity, can modulate arthritogenic response in adjuvant arthritis. Regulatory mechanisms induced by Hsp60, Hsp70, and Hsp90 are reinforced by an immune network that connects their reactivities.
- cell lines that contain human tumor-derived temperature-sensitive p53 mutants show that Hsp90 is required for both stabilization and reactivation of mutated p53 at the permissive temperature
- the Hsp90.Cdc37 molecular chaperone module has a central role in interleukin-1 receptor-associated-kinase-dependent signaling by toll-like receptors
- Hsp90 is involved in hsp70 mRNA stabilisation and the HSF1 activation can be suppressed by high hydrostatic pressure
- Hsp90-Akt forms a complex with ASK1 and protect vascular endothelium from stress-induced apoptosis.
- Data suggest that HSP90 induces efficient activation of N-WASP downstream of phosphorylation signal by Src family kinases and is critical for N-WASP-dependent podosome formation and neurite extension.
- S-nitrosylation may functionally regulate the general activities of Hsp90 and provide a feedback mechanism for limiting endothelial nitric oxide synthase activation.
- inhibition of Hsp90 leads to ZAP-70 degradation, apoptosis, and impaired signaling
- Component of the c-Ha-ras ARE/EpRE heterocomplex. We conclude that both internal bases and flanking sequences regulate nuclear protein recruitment and complex assembly.
- association of Hsp90 with ClC-2 results in greater channel activity due to increased cell surface channel expression, facilitation of channel opening, and enhanced channel sensitivity to intracellular [Cl-]
- Sp1 interacts with Hsp90alpha to recruit it to the promoter of 12(S)-lipoxygenase and then to regulate gene transcription by modulating the binding ability of Sp1 to promoters
- Nuclear magnetic resonance study of binding to CDC37.
- The function of Hsp90alpha is impaired by the Q488H polymorphism.
- By applying co-immunoprecipitation with endogeneous Hsp90, there were identified 39 novel protein interaction partners of this chaperone in human embryonic kidney cells (HEK293).
- HSF1 phosphorylation by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding
- JAK1/2 are client proteins of Hsp90 alpha and beta; Hsp90 and CDC37 play a critical role in types I and II interferon pathways
- The aberrant expression of ZAP-70 in more aggressive forms of chronic lymphocytic leukemia requires the chaperoning action of activated heat-shock protein 90, which may be specifically inhibited by the therapeutic strategies discussed in this review.
- Chk1 is post-translationally chaperoned to an active kinase. This reaction minimally requires Hsp90, Hsp70, Hsp40, Cdc37, and the protein kinase CK2.
- The present study identified a specific interaction between IRF3 and chaperone heat-shock protein of 90 kDa (Hsp90).In addition, TBK1 is found to be a client protein of Hsp90 in vivo.
- Complex formation between Hsp90 and p23 increases the apparent affinity of Hsp90 for ATP analogue adenylyl imidodiphosphate (AMP-PNP) and completely inhibits ATPase activity.
- GCUNC-45 is a novel modulator of progesterone receptor chaperoning by hsp90.
- Hsp90 is required for translocation of FGF-1 and FGF-2 across the endosomal membrane
- We report the solution structure of a complex of the TPR domain of Ppp5 with the C-terminal pentapeptide of Hsp90.This may be important for the relief of autoinhibition in Ppp5 and for the mechanisms of TPR-mediated recognition of Hsp90 by other proteins
- p23 forms a specific complex with Hsp90 primarily through binding to its middle domain
- inhibition of the hsp90-dependent trafficking mechanism prevents aggregation of the expanded glutamine androgen receptor
- This is the first report identifying caspase-3 as a substrate protein of Hsp90.
- Heat shock protein 90 physically interacts with HGTD-P.
- Stimulation of ARO cells with specific nucleotide receptors agonists evidenced a major involvement of P2Y1 and P2Y2 receptors in controlling the Hsp90 activation.
- Increased expression of HSP90 Heat-Shock Proteins is associated with colon cancer
- Hsp90 inhibition transiently activates Src kinase and promotes Src-dependent p85 PI3K and Akt and Erk activation
- Analysis of expression of HSP90 and the efects of its inhibitor 17-AAG in multiple myeloma
- These findings indicate that parasite-induced IkappaB kinase (IKK) activity does not require functional Hsp90.
- The data shows the expression and purification of an Hsp90-Cdc37-Cdk4 complex, defining its stoichiometry, and determining its 3D structure by single-particle electron microscopy.
- HSP90 binding to ErbB2 participates in regulation of src kinase activity as well as kinase stability
- Our data demonstrate for the first time that 17-AAG inhibits the HR repair process and could provide a new therapeutic strategy to selectively result in higher tumor cell killing.
- As described in this review, in contrast to other targets where cancer might escape inhibition via alternative pathways, HSP90 operates at multiple checkpoints in a genitourinary cancer cell.
- Hsp90 and PARP-1 bind to TonEBP; PARP-1 expression reduces TonEBP transcriptional activity and the activity of its
- The basal levels of Hsp32, Hsp70 and Hsp90 increased significantly with age in controls. Higher levels of Hsp32, Hsp70 and Hsp90 were noticed in patients with inflammation.
- These data suggest that acetylation/deacetylation of K294 plays an important role in regulating the Hsp90 chaperone cycle.
- These findings raise the possibility that ZAP-70 may serve as an important link between GC and TcR-induced signaling, thereby transmitting non-genomic GC action in T-cells.
- the antineoplastic activity of bortezomib depends on cell-cell contact between DCs and dying tumor cells and is mediated by bortezomib-induced exposure of heat shock protein 90 (hsp90) on the surface of dying cells
- These data implicate a central role for Hsp90 in the development of Alzheimer's disease and other tauopathies.
- DAPK is found in two distinct immune complexes, one containing HSP90 and CHIP and a second complex containing only DIP1/Mib; strict modulation of DAPK activities by HSP90 heterocomplexes is critical for regulation of apoptosis and cellular homeostasis
- Hsp90 promotes activation of the Fanconi anemia pathway through regulation of intracellular turnover and trafficking of FANCA
- ARs having a Leu701His mutation AR(L701H) was highly dependent on Hsp90 for its hormone-independent activation, suggesting that this chaperone functions in AR(L701H) folding.
- Stat1 in complex with Stat3 and HSF1 bound at the GAS element led to a moderate heat shock induction, designated as an "intrinsic" induction of the hsp90alpha gene; a changed level of heat shock induction was also controlled by the Stat1 on hsp90alpha.
- Hsp90 inhibition significantly inhibited DC function.
- FKBP38 is a co-chaperone of HERG and contributes via the Hsc70/Hsp90 chaperone system to the trafficking of wild type and mutant HERG potassium channels
- This study reveals a novel role of Hsp90 in the signaling events mediated by a G protein-coupled receptor.
- the staurosporine-induced death pathway bifurcates in caspase-compromised cells and commitment to apoptotic or necrotic phenotypes depends on cathepsin protease or Hsp90 chaperon activities.
- The present data denote Hsp90-Cdc37 as a transiently acting essential regulatory component of IKK signaling.
- We review the contemporary body of knowledge regarding the biochemical mechanisms of Hsp90 and update the most current paradigms defining its involvement in both normal and pathological cell physiology. [review]
- Hsp90 dimerization is required for in vivo function
- During mitosis, HSF2 is bound to the HSE promoter elements of other heat shock genes, including hsp90 and hsp27, and the proto-oncogene c-fos. The presence of HSF2 is important for expression of these genes.
- Hsp90-directed chaperones are regulators of mitochondrial integrity, and their organelle-specific antagonists may provide a previously undescribed class of potent anticancer agents.
- Hsp90 inhibition decreases mitochondrial protein turnover
- Blocking Hsp90 disrupts IGF-I and IL-6-induced proangiogenic signaling cascades by targeting IGF-IR and STAT3 in pancreatic cancer
- exercise-heat acclimation resulted in increased baseline levels of HSP72 and HSP90; ex vivo heat inducibility of HSP72 was blunted after heat acclimation
- HSP90 stabilizes c-Jun protein, and so increases the total activity of c-Jun in HEK293 cells.
- HSP90 expression was significantly higher in tumors than nevi and was associated with disease progression
- Overall, these results indicate that HDAC6 and HDAC10 play important roles in Hsp-mediated VEGFR regulation.
- A side-by-side comparison of the Hsp90-dependent chaperoning of Chk1 to that of the progesterone receptor (PR) was performed to show that these distinct types of clients have different chaperoning requirements.
- inhibitory effect on uveal melanoma cells using an Hsp90 inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), in uveal melanoma cell lines.
- Our results identify a new role for HSP90 in protein sorting, pointing to a central role for this molecular chaperone in the cell.
- GCUNC45 is required for the normal cellular distribution of Hsp90beta, but not Hsp90alpha.
- High expression levels of HSP90 are associated with non-small cell lung cancer
- GDNF reverses this ethanol-mediated adaptation by inhibiting the interaction of tyrosine hydroxylase with HSP90
- The predicted pocket is formed by two grooves located between helix H18, the loop downstream of H18 and the loop connecting helices H20 and H21 of each monomer of the C-terminal domain, with only two amino acids contributing from each middle domain.
- Results suggest that HSP90 is overexpressed in poor-prognosis acute myeloid leukemia cells and plays a role in cell survival and resistance to chemotherapy.
- conformational analysis of hydrolysis by human Hsp90alpha and Hsp90beta
- Tah1 is specific for Hsp90, and is able to bind tightly the yeast Hsp90, and the human Hsp90alpha and Hsp90beta proteins, but not the yeast Hsp70 Ssa1 isoform
- It is likely that Hop binds to both monomers of Hsp90 in the form of a clamp, interacting with residues in the middle domain of Hsp90, preventing ATP hydrolysis, possibly by the preventing binding of N-terminal and middle domains in Hsp90 monomers.
- Overexpression of hsp90 is associated with colorectal cancer progression.
- The present study agrees with the experimental structural data and provides a plausible molecular model for understanding mechanisms of modulation of molecular chaperone activities by binding partners.
- These data reveal an essential level of TGFbeta signaling regulation mediated by Hsp90.
- Hsp90N was created as an artifact of a cDNA synthesis or that it is a chimeric protein, being a result of the chromosomal rearrangement that occurred in a single cell line, after this line was established.
- Overexpression of telomerase-associated hsp90/p23 proteins are prostatic intraepithelial neoplasia and carcinomas
- HSP90 inhibition abrogates the topoisomerase I poison-induced G2/M checkpoint in p53-null tumor cells by depleting CHK1 and WEE1.
- physical interaction between hsp90 and the hTERT promoter occurs in telomerase-positive cells but not in normal human cells and is necessary for the enhanced hTERT expression and telomerase activity in cancer cells
- Data show that Hsp90 is an inclusion body components in neuronal intranuclear inclusion disease identified by anti-SUMO-1-immunocapture.
- These data reveal a cyclic regulatory mechanism for Cdc37, in which its constitutive phosphorylation is reversed by targeted dephosphorylation in Hsp90 complexes.
- This study proposes that extracellular HSP90 would contribute to IL-8 elevation in the stressed vasculature, and that TLR-4, mitogen-activated protein kinases, NF-kappaB, and reactive oxygen species are involved in that process.
- Hsp90 overexpression correlates with several adverse parameters for gastrointestinal stromal tumors. Hsp90alpha seems more relevant to the aggressiveness of gastrointestinal stromal tumors than Hsp90beta
- These data support a conserved three-state chaperone cycle where the conformational equilibrium varies between species, implicating evolutionary tuning to meet the particular client protein and metabolic environment of an organism.
- Data show that Hsp90 acts as a regulator of pathogenic changes that lead to the neurodegenerative phenotype in Alzheimer's disease.
- This protein has been found differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
- Heat shock protein 90 inhibitors suppress aryl hydrocarbon receptor-mediated activation of CYP1A1 and CYP1B1 transcription and DNA adduct formation.
- Upregulation of HSP90 Heat-Shock Proteins is associated with squamous cell carcinoma in oesophageal cancer.
- Both rab11a and HSP90 appear to be involved in the process of exocytosis of internalized extracellular alpha-synuclein.