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Validated All-in-One™ qPCR Primer for HSP90B1(NM_003299.2) Search again
Product ID:
HQP110827
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ECGP, GP96, GRP94, HEL-S-125m, HEL35, TRA1
Gene Description:
heat shock protein 90 beta family member 1
Target Gene Accession:
NM_003299.2(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. HSP90B1 is an endoplasmic reticulum HSP90 protein. Other HSP90 proteins are found in cytosol (see HSP90AA1; MIM 140571) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM].
Gene References into function
- a paper describing a pathway in which this gene product functions
- associated with HBV polymerase in human liver cell HepG2
- OmpA of E. coli K1 interacts with a gp96-like molecule on HBMECs for invasion (Ecgp: 96-kDa human brain microvascular endothelial cell (HBMEC) glycoprotein)
- Heat shock protein 96 purified from melanoma or liver metastases of colon carcinoma cells contains immunogenic peptides that can be presented to CD8+ T cells and can activate them both in vitro and in vivo.
- Orientia tsutsugamushi down-regulated gp96 an endothelial cell line, HMEC-1.
- Expression of GRP94 suppressed A23187-induced apoptosis and stabilized calcium homeostasis.
- In patients with cholangiocellular carcinoma, the presence of cells expresing Grp94 is related to CD83-positive dendritic cells.
- The glucose-regulated protein (GRP94) is upregulated in human endothelial cells in response to hypoxia by HIF-1.
- HSP70 and grp94 express differently in cell plasma and nuclei. The expression intensity of HSP70 is related to the differentiation of esophageal carcinoma.
- Results strongly argue against a regular role for gp96 as a peptide chaperone in antigen processing.
- GRP94 is highly expressed in human gastric carcinoma BGC-823 cells through the whole cell cycle.
- Gp96 is exploited by Listeria monocytogenes as a receptor for cell invasion or signalling events that may interfere with the host immune response in the course of Listeria infection.
- Heat shock protein 90beta (Hsp90beta)-bound activated tyrosine kinase Ack1 and treatment of cells with geldanamycin, a Hsp90 inhibitor, inhibited Ack1 kinase activity and suppressed prostate tumorigenesis.
- These results suggest that CYP2E1 mediated oxidative stress downregulates the expression of GRP proteins in HepG2 cells and oxidative stress is an important mechanism in causing ER dysfunction in these cells.
- It was found that in vitro these proteins were capable of maturating human monocyte-derived dendritic cells (MDDC) isolated from healthy donors as well as from HBV-positive, hepatocellular carcinoma (HCC) patients.
- TLR2 and TLR4 ligand interaction with the N-terminal domain of Gp96 amplifies innate and adaptive immune response
- TLR4 signaling to lipopolysaccharide can be positively enforced by expressing gp96 on cell surfaces through the chaperone function of, but not the direct signaling by, transgenic gp96.
- ICMT inhibition induces endothelial cell apoptosis through GRP94
- Retention of amyloidogenic mutant TTRs induced the unfolded protein response and upegulated the expression of GRP94.
- NTN4, TRA1, and STC2 have roles in progression of breast cancer
- These results suggest that a novel mechanism other than endoplasmic reticulum(ER) stress element-dependent mRNA transcription is required for induction of GRP94 and phosphorylation of PKR contributes to the induction of GRP94 under ER stress.
- Immunohistochemical analysis showed highly expressed Grp94 in primary OSCCs (oral squamous cell carcinoma). Grp94 may have potential clinical application as a novel diagnosis and prognostic biomarker for human OSCCs.
- HSP90B1 may have a pathophysiological role in bipolar disorder in the Japanese population.
- results indicate a significant correlation between the immunopositivity of HSP72 and gp96 and the progression of colonic carcinomas
- Heat shock protein 90beta1 is essential for polyunsaturated fatty acid-induced mitochondrial Ca2+ efflux
- We found higher expression of gp96 protein in breast carcinoma cells and low or no expression in normal breast cells.
- OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
- These data indicate that HCV E2 blocks apoptosis induced by HCV infection and the host immune system through overproduction of GRP94, and that HCV E2 plays an important role in persistent HCV infection.
- We could demonstrate an association of GRP78 and GRP94 mRNA and protein expression with tumor stage and behaviour in esophageal adenocarcinomas.
- the novel involvement of GRP94 suppression in prostate cancer metastasis.
- We conclude that human colonocyte gp96 serves as a plasma membrane binding protein that enhances cellular entry of Clostridium difficile toxin A (TxA), participates in cellular signaling events in the inflammatory cascade, and facilitates cytotoxicity.
- Up-regulated expression of GRP78 and GRP94 was possibly involved in pathogenesis, growth, invasion, and metastasis of gastric carcinomas.
- Grp94 with IgG promoted the angiogenic differentiation in HUVECs.
- Data show that Stat3 activation and its interaction with Ec-gp96, which in turn interacts with E. coli outer membrane protein A, are critical for E. coli invasion.
- Interaction of gp96 with CD91 is a productive event that directly and specifically triggers functional responses in plasmacytoid dendritic cells.