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Validated All-in-One™ qPCR Primer for HSPA1A(NM_005345.5) Search again
Product ID:
HQP009077
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HEL-S-103, HSP70, HSP70-1, HSP70-1A, HSP70-2, HSP70.1, HSP70.2, HSP70I, HSP72, HSPA1
Gene Description:
heat shock protein family A (Hsp70) member 1A
Target Gene Accession:
NM_005345.5(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
This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq].
Gene References into function
- No variation in Hsp70 mRNA level during cardiac surgery in pediatric patients evaluated by semiquantitative RT-PCR
- Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1
- Effect of hyaluronan oligosaccharides on the expression of heat shock protein 72.
- These data strongly suggest that in TNF-induced apoptosis, Hsp72 specifically interferes with the Bid-dependent apoptotic pathway via inhibition of JNK.
- IL-6 activates HSP72 gene expression in human skeletal muscle.
- These observations suggest that heat shock protein 72 functions as an endogenous inhibitor of ASK1.
- Increase in arterial HSP72 was accounted for, at least in part, by release from the hepatosplanchnic viscera with values increasing (P < 0.05) from undetectable levels at rest to 5.2 +/- 0.2 pg min(-1) after 120 min.
- HSP72 may protect intestinal epithelial cells from Clostridium difficile toxin A-mediated damage through actin stabilization, mitochondrial protection, and inhibition of apoptosis activation, but not by prevention of RhoA glucosylation.
- lipid rafts are part of a mechanism ensuring the correct functions of Hsp70
- in very low birth weight neonates carrying HSP72 (1267)GG genetic variation, which is associated with low inducibility of HSP72, the risk of of acute renal failure was increased
- Basal expression of both HSP72 and HO-1 mRNA were lower (P < 0.05) by 33 and 55%, respectively, when comparing diabetic patients with age-matched and young control subjects
- cytoplasmic localization of Hsp72 might be correlated with the development of thermotolerance
- HSP-72 gene expression at the time of engraftment does not play a role in graft protection.
- These data demonstrate that the human brain is able to release Hsp72 in vivo in response to a physical stressor such as exercise.
- the mesothelial stress response confers cytoprotection in experimental peritoneal dialysis, mediated by the induction of HSP-72
- Ability of Hsp72 to inhibit Fas-mediated apoptosis is limited to type II cells where involvement of the intrinsic pathway is required for efficient effector caspase activation.
- results show hsp70i bookmarking is mediated by HSF2 which binds this promoter in mitotic cells, recruits protein phosphatase 2A & interacts with the CAP-G subunit of condensin to promote dephosphorylation & inactivation of condensin complexes
- downregulation of Hsp72 leads to severe suppression of the major survival pathways, ERK and NF-kappaB, which may be responsible for enhanced sensitivity of prostate carcinoma cells to a variety of anticancer treatments
- L-glutamine potentiation of Hsp72 is associated with increased epithelial resistance to apoptotic injury.
- EndoG forms complexes with AIF and FEN-1 but not with PCNA. Heat shock proteins 70 interact with EndoG and are involved in the regulation of its activity.
- Hsp70 blocks heat-induced apoptosis primarily by inhibiting Bax activation and thereby preventing the release of proapoptotic factors from mitochondria
- Our results indicate that pro-apoptotic activity of quercetin may be correlated not only with the inhibition of Hsp72 expression but also with suppression of its migration to the nucleus.
- Up-regulation of HSP70 Heat Shock Protein is associated with hepatocellular carcinoma
- These result suggest that overexpression of HSP70 plays an important role in protecting gastric cells against NH(2)Cl-induced injury.
- HSP25 and HSP70i activate HSF1 and have roles in inhibition of ERK1/2 phosphorylation
- During exercise, with and without carbohydrate ingestion, plasma HSP72 increased 5-fold. The concentrations of HSP72 in CSF did not change with exercise and was below the corresponding plasma level.
- eHsp72 was present in plasma and pulmonary edema (PE)fluid of ALI patients and it was significantly higher in PE fluid from patients with preserved alveolar epithelial fluid clearance. eHsp72 may serve as a marker of SPR activation of ALI patients.
- applied a genetic-demographic approach to a dataset relevant to two genes, APOE and HSP70.1, previously shown to be related to longevity by the gene-frequency method
- Upon heat shock, the Hsp70.1 promoter-bound PARP-1 is released to activate transcription through ADP-ribosylation of other Hsp70.1 promoter-bound proteins.
- This data indicates a tumor-specific expression of hsp70, but does not support its relevance in the DC cross-presentation of TAs.
- EDTA-treated blood was significantly higher in Hsp72 concentration than all other treatments (P < or = 0.001), whilst heparin plasma (LH) was significantly higher than serum derived on ice (SI) and at room temperature (SR) .
- Hsp72 provides a selective advantage to cancer cells by suppressing default senescence via p53-dependent and p53-independent pathways.
- identification of the most common polymorphisms in HSPA1A & HSPA1B in asthmatics & controls from 3 ethnic groups; study indicates most of the HSPA1A and HSPA1B polymorphisms identified in dbSNP are rare or were derived during post transcriptional events
- HSPA1A is an important regulator of the stability and function of ZNF198 and its oncogenic derivative, ZNF198-FGFr1.
- HSP70-1+190G/C may affect susceptibility to ischemic stroke (IS) and smoking along with HSP70-1+190G/C may increase the risk of IS.
- Acetylglucosamine (GlcNAc) level and Hsp70-GlcNAc-binding activity (HGBA) behaviour after exposure of HeLa and HepG(2) cells to a wide variety of stresses, was investigated.
- HSP70-1 polymorphism is not associated with type-1 diabetes mellitus in a group of African Americans.
- activation of HSF1 and stabilization of Bcl-X(L) mediate a protective response that may contribute significantly to the cellular biology of lipid peroxidation
- exercise in hot conditions produced no significant increases in HSP72 expression in skeletal muscle compared to exercise in cold conditions
- Both Hsp70B' and Hsp72 are important for maintaining viability under conditions that increase the accumulation of damaged proteins in HT-29 cells.
- Hsp60 and Hsp72 activation and inflammatory markers were correlated with the extent of cardiac and microvascular dysfunction in patients with angiographycally normal coronary arteries.
- exercise-heat acclimation resulted in increased baseline levels of HSP72 and HSP90; ex vivo heat inducibility of HSP72 was blunted after heat acclimation
- results indicate a significant correlation between the immunopositivity of HSP72 and gp96 and the progression of colonic carcinomas
- The A-110C polymorphism of HSP70-1 may be associated with OAG pathogenesis in Japanese patients.
- main finding of this study was the down-regulation of Hsp72 as well as the protective effect against oxidative damage accumulation in relatively higher levels of physical activity during aging
- human blood ozonation induces a remarkable upregulation of heme oxygenase-1 and heat stress protein-70
- endogenously produced and released extracellular Hsp72 has the ability to reprogram the in vitro response to endotoxin in cultured human mononuclear cells
- GRP-induced up-regulation of Hsp72 promotes CD16+/94+ natural killer cell binding to colon cancer cells causing tumor cell cytolysis.
- higher expression of HSPA6 & HSPA1A was exhibited in placental vascular disease (PVD)subjects compared to normal pregnancy; significant upregulation of HSP70 mRNA & protein in placental tissue & microvascular endothelial cells of PVD subjects was observe
- DJ-1 inactivation may promote alpha-syn aggregation and the related toxicity, and in this model HSP70 is involved in the antioxidant response and in the regulation of alpha-syn fibril formation
- HSP72 was associated with CD44v6 precursor fragments in human colonic carcinoma cells. The interaction between HSP72 and CD44v6 in human colonic carcinoma cells may contribute to study the pathogenesis and immunotherapy of colonic carcinoma.
- Results suggest that the parthenolide-induced apoptosis of A549 cells is due to the direct suppression of NF-kappaB activity in a p53- and hsp72-independent manner based on NF-kappaB signaling.
- Human HSP72 binds to TLR2 and TLR4 on murine hepatocytes and signals through NF-kappaB to increase MIP-2 production.
- Hsp70B' and Hsp72 play cooperative roles in cell survival of proteotoxic stress.
- eHsp72 is a function of the core temperature attained rather than the rate of heat storage.
- This article describes the Hsp 72 response to exercise in relation to the tissue assayed (i.e. skeletal muscle vs lymphocyte) and the origin of the sample (i.e. venous vs arterial serum) [review]
- Simultaneously reducing the expression of both HSC70 and HSP72 induces proteasome-dependent degradation of HSP90 client proteins, G1 cell-cycle arrest, and extensive tumor-specific apoptosis in human tumor cell lines.
- Mild electrical stimulation increases ubiquitinated proteins and Hsp72 in A549 cells via attenuation of proteasomal degradation.
- Experiments using alpha-Syn deletion mutants indicated that interactions between the Hsp70 substrate binding domain and the alpha-Syn core hydrophobic region underlie assembly inhibition.
- Hsp72 is intimately involved in suppression of at least two separate senescence signaling pathways that are regulated by distinct oncogenes in transformed cells
- Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.