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Validated All-in-One™ qPCR Primer for HSPA9(NM_004134.6) Search again
Product ID:
HQP009088
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
CRP40, CSA, EVPLS, GRP-75, GRP75, HEL-S-124m, HSPA9B, MOT, MOT2, MTHSP75, PBP74, SAAN, SIDBA4
Gene Description:
heat shock protein family A (Hsp70) member 9
Target Gene Accession:
NM_004134.6(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:
Summary
The product encoded by this gene belongs to the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate proteins. This gene encodes a heat-shock cognate protein.
Gene References into function
- Implication of PBP74/mortalin/GRP75 in the radio-adaptive response.
- Cytoplasmic sequestration and inactivation of p53 by mot-2 occurs by its binding to the cytoplasmic sequestration domain;perturbation of mot-p53 interactions can be employed to abrogate cytoplasmic retention of wild-type p53 in tumors.
- Results demonstrate that mot-2 and telomerase can cooperate in the immortalization process.
- Unexpected extracellular location and characteristic biological function of Grp94 even at a late stage of type 1 diabetex.
- Mortalin and HSP60 interact both in vivo and in vitro, and that the N-terminal region of mortalin is involved in these interactions.
- attempted to disrupt mot-2-p53 interactions by overexpression of short p53 carboxyl-terminal peptides
- Taken together, GRP78/75 and RHAMM complexes may stabilize microtubules in the interphase, associated with a downregulation of RHAMM. These results reveal a new biochemical activity of RHAMM.
- Overexpression of mortalin was sufficient to increase the malignancy of breast carcinoma cells. This study demonstrates that upregulation of mortalin contributes significantly to tumorigenesis, and thus is a good candidate target for cancer therapy.
- Findings not only identify mortalin as an upstream molecule of p53 but also provide evidence for the involvement of centrosomally localized p53 in the regulation of centrosome duplication.
- We propose that the differential regulation of mortalin in AD and by the APOE genotype is a cellular defense mechanism responding to increases in oxidative stress.
- review of mortalin involvement in cellular senescence from the perspective of its mitochondrial import, chaperone, and oxidative stress management functions [mortalin]
- Mortalin binds to Mps1, and is phosphorylated by Mps1 on Thr62 and Ser65
- data suggest that mortalin is involved in the mediation of EPO signaling and plays an important role in stimulating the growth of erythroid progenitor cells
- Mortalin (HSPA9) is associated with hepatocellular carcinoma metastasis and thus suggested as a tumor marker for predicting early recurrence.
- mortalin, a mitochondrial protein, was decreased in the parkinson disease progression.
- aptitude to impact on mitochondrial function and homeostasis; its interfacing energy metabolic functions with synaptic plasticity, and modulation of brain aging via the cellular senescence pathways
- GRP75 has an essential role in the differentiation of neuroblastoma
