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Validated All-in-One™ qPCR Primer for AIFM1(NM_004208.3) Search again
Product ID:
HQP022136
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AIF, AUNX1, CMT2D, CMTX4, COWCK, COXPD6, DFNX5, NADMR, NAMSD, PDCD8, SEMDHL
Gene Description:
apoptosis inducing factor mitochondria associated 1
Target Gene Accession:
NM_004208.3(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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Summary
This gene encodes a flavoprotein essential for nuclear disassembly in apoptotic cells that is found in the mitochondrial intermembrane space in healthy cells. Induction of apoptosis results in the translocation of this protein to the nucleus where it effects chromosome condensation and fragmentation. In addition, this gene product induces mitochondria to release the apoptogenic proteins cytochrome c and caspase-9. Several alternative transcripts encoding different isoforms have been identified for this gene. [provided by RefSeq].
Gene References into function
- observations suggest that AIF-induced nuclear apoptosis requires a direct interaction with DNA
- These data suggest that apoptosis-inducing factor (AIF) is expressed in human coronary artery endothelial cells (HCAECs) and is upregulated by oxidized low density lipoproteins.
- Possible contribution of apoptosis-inducing factor and reactive oxygen species to UVB-induced caspase-independent cell death in the T cell
- apoptosis-inducing factor has a role in oxidant-induced cell death in retinal pigment epithelium cells
- AIF is not implicated in CD47-dependent cell death of T cells
- AIF and CYPA cooperate in apoptosis-associated chromatinolysis.
- endonuclease G and apoptosis-inducing factor are relocated and have roles in calcium induced signaling and oxidative stress-related impairment of mitochondria
- suggests a role in mitochondrial-mediated death pathway
- The oxidoreductase function of AIF is required for the maintenance of glutathione levels in stress conditions and that glutathione is a major regulator of SG.
- AIF plays a role in oxidative phosphorylation
- AIF is involved in NMDA- and kainic acid- but not AMPA-induced excitotoxicity. AIF plays an important role in both BAX-dependent and BAX-independent mechanisms of neuronal injury.
- findings indicate that PARP-1 activation and a PARP-1-dependent, caspase-independent, nuclear translocation of AIF contribute to apoptotic cerebral endothelial cell death after ischemia-reperfusion
- AIF is responsible for stage I nuclear morphology and HMW DNA degradation is a caspase-activated DNase and AIF-independent process
- AIF short (AIFsh), a new pro-apoptotic isoform of AIF, reveals that the first N-terminal 352 amino acids of AIF are not required for its apoptotic activity.
- AIF-mediated cell death is regulated by the functional interplay of SIRT1 and PARP-1 in response to DNA damage
- the cloning and the biochemical characterization of a new isoform named AIF short 2 (AIFsh2)
- Moreover, in the absence of overt apoptotic signals, the constitutive induction of AIF by p53 may underpin a cytoprotective maintenance role, based on the role of AIF in ensuring proper mitochondrial function.
- AIF overexpression specifically resulted in the activation of caspase-7, thereby amplifying the inhibition of protein
- Hypochlorous acid induced Bax-dependent mitochondrial permeability which led to cell death without caspase activity by processes involving AIF/EndoG-dependent pathways.
- study of cellular localization of the endonuclease G, AIF & AMID during apoptosis using bioinformatics and image analysis
- Down-regulation of hSUV3 results in cell cycle perturbations and in apoptosis, which is both AIF- and caspase-dependent, and proceeds with the induction of p53.
- PKB/Akt inhibits ceramide-induced apoptosis in neuroblastoma cells by blocking AIF translocation.
- Data suggest that erythroblast chromatin degradation may involve caspase activated DNase and apoptosis inducing factor, enzymes distinct from those active in apoptotic cells.
- AIF is associated with cisplatin induced apoptosis in prostate cancer
- Inhibitor of apoptosis proteins, nuclear factor-kappa, Smac/DIABLO and apoptosis inducing factor were increased in colon cancer cells.
- TULA enhances the apoptotic effect of AIF by facilitating the interactions of AIF with its apoptotic co-factors
- Scythe regulates apoptosis-inducing factor stability during endoplasmic reticulum stress-induced apoptosis
- Hibiscus syriacus extract exhibits a cytotoxic effect on lung cancer cells by activation p53 and AIF.
- Promoting neuronal survival of GDNF might be related to the reduction of AIF nuclear translocation, indicating the high therapeutic potency of SeV/GDNF for cerebral ischemia.
- These results provide novel insights into the mechanism of AIF release during cell death.
- AIF translocation has a role in FK228-induced autophagy in malignant rhabdoid tumor cells
- AIF is essential for maintaining beta-cell mass and for oxidative stress response.