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Validated All-in-One™ qPCR Primer for HSPA4(NM_002154.3) Search again
Product ID:
HQP009081
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
APG-2, HEL-S-5a, HS24/P52, HSPH2, RY, hsp70, hsp70RY
Gene Description:
heat shock protein family A (Hsp70) member 4
Target Gene Accession:
NM_002154.3(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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Gene References into function
- induction and expression analysis after heat and physical exercise, transcriptional, protein expression, and subcellular localization
- 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.
- APG-2 has a chaperone-like activity similar to Hsp110 and is overexpressed in human hepatocellular carcinoma.
- stress proteins in subcellular structures of cancer cells exposed to heat shock
- 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.
- Polymorphism of the HSP70-hom gene is associated with the development of posttransplant complications. Recipient HSP-AA homozygous genotype is a risk factor for acute graft-versus-host disease
- This study suggests that Hsp70 and Hsp90 are closely related to cytoprotection of RPE cells in response to protein phosphatase inhibition.
- specific down-regulation of HSP70 in KATO III cells occurred only in the presence of live Helicobacter pylori; a novel regulatory mechanism for H. pylori-induced HSP70-dependent apoptosis in the human gastric epithelial cell line is proposed
- Human keratinocyte-derived cells release Hsp70 in the extracellular medium through a pathway involving secretory-like granules.
- Acidic pH exposure protects HEMEC through induction of Hsps and activation of MAPK and PI3 kinase pathway.
- Results showed HSP70 expression was inhibited in Helicobacter pylori infected MKN7 cells.
- The binding of Hsp70 with PreAS only requires the substrate-binding subdomain, and the binding with AS nuclei requires the C-terminal lid subdomain as well.
- Coexpression of the chaperone protein Hsp70, causes alpha-synuclein to adopt a different, open conformation, but Hsp70 does not alter alpha-synuclein-alpha-synuclein interactions.
- Plasminogen bound to hsps 27, 60, and 70 and Angiostatin predominantly bound to hsp 27 and to hsp 70 in a concentration- and kringle-dependent manner.
- 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.
- Our results suggest that the widespread accumulation of Hsc70 and Hsp70 may occur in brains with MSA, and that Hsc70 and Hsp70 may be associated with the pathogenesis of MSA.
- All of the breast cell lines examined showed Hsp70 surface expression. These results also confirm previous studies, demonstrating that Hsp70 is on the plasma membrane of tumor cell lines.
- These findings suggest that in tumors retaining functional p53 and expressing high levels of Hsp70, TRAIL may be an effective therapy.
- data suggest that blood cardioplegia can induce an increment in the expression of hsp70-1, confirming its protective role in ischemia/reperfusion injury.
- HSP60 and HSP70 released upon tissue damage might play a role in the regulation of bacteria-induced inflammation
- Authors hypothesized that differing relations between surface expression of Hsp70 on tumor cells and clinical outcomes may reflect differences in the route of metastases.
- HSP70-mediated inhibition of apoptosis seems to be of minor importance for carcinogenesis and tumor progression in renal cell carcinomas.
- Results indicate that miR-1 and miR-133 are involved in regulating cell fate, and that post-transcriptional repression of HSP60 and HSP70 by miR-1 and of caspase-9 by miR-133 contributes significantly to their opposing actions.
- Results suggest that the individuals with the homozygous HSP70-1 C/C genotype among the coke-oven workers may be susceptible to DNA damage.
- HSP70 gene expression tended to be induced in the group administered Healing and Wound Emulsion following gamma-ray irradiation.
- The degradation of Hsp70 was significantly reduced in TAT-Hsp40-containing cells as a consequence of reduced ubiquitin-proteasome activity after oxidative injury.
- Hsp70 cell surface and mRNA expression was studied in K562, Jurkat and CCRF-CEM human leukemia cell lines
- Hsp70 interaction with membranes acts as a platform for its release into the extracellular environment during its recovery from stress.
- Sequential measurement intraoperatively of the levels of the heat shock proteins HSP70 and HSP27 in the cerebrospinal fluid can predict those patients who are at greatest risk for paralysis during thoracic aneurysm surgery.
- PHAPI, CAS, and Hsp70 function together to accelerate nucleotide exchange on Apaf-1 and prevent inactive Apaf-1/cytochrome c aggregation.
- these data suggest that the IkappaB-alpha/NF-kappaB pathway has a critical role in the partial maturation of dendritic cells induced by recombinant HSP70.
- These results suggest that aging-related changes in basal Hsp70 levels in peripheral blood lymphocyte are linked to the altered frequency of lymphocyte subsets and not to increases in aged lymphocytes per se.
- Hsp70 was isolated as a putative Rictor interacting protein.
- The structure of an Hsp110:Hsc70 nucleotide exchange complex, is reported.
- The newly discovered interaction between HBP21 and Hsp70 suggests that HBP21 may be involved in the inhibition of progression and metastasis of tumor cells.
- Hsp70 gene expression in Rheumatoid Arthitis-affected synovial tissue is followed by Hsp70 cell surface expression on fibroblast-like synovial cells growing from RA synovial tissue.
- mRNA expressions of Hsp70, Hsp32 and Bax significantly increased in mononuclear blood cells after marathon running, whereas Hsp27 and Bad mRNA expression levels showed no significant changes.
- mitochondrial ribosomal protein S12 3'-UTR interacts specifically with TRAP1 (tumor necrosis factor receptor-associated protein1), hnRNPM4 (heterogeneous nuclear ribonucleoprotein M4), Hsp70 and Hsp60 (heat shock proteins 70 and 60), and alpha-tubulin
- Serum Hsp70 (heat shock protein 70)levels were increased in Systemic sclerosis patients, and associated with pulmonary fibrosis, skin sclerosis, renal vascular damage, oxidative stress, and inflammation
- Hsf1 is required for p53 nuclear importation and activation, which implies that heat shock factors play a role in the regulation of p53.
- Serum levels of free heat shock protein 70 and anti-HSP70 are elevated in Behcet's disease