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C12orf5 is regulated as part of the p53 tumor suppressor pathway and encodes a protein with sequence similarity to the bisphosphate domain of the glycolytic enzyme that degrades fructose-2,6-bisphosphate. Additionally we are shipping Chromosome 12 Open Reading Frame 5 Antibodies (109) and Chromosome 12 Open Reading Frame 5 Kits (3) and many more products for this protein.
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Human C12orf5 Protein expressed in Escherichia coli (E. coli) - ABIN667299
Bensaad, Cheung, Vousden: Modulation of intracellular ROS levels by TIGAR controls autophagy. in The EMBO journal 2009
Show all 2 references for ABIN667299
TIGAR expression may be used as a bio-marker for detection of colorectal cancer and can be used as a target for developing therapeutics for the treatment of colorectal cancer.
TIGAR knockdown reduced tumor growth rate.
Geranylgeranoic acid induced upregulation of the TIGAR gene, which might inhibit the glycolysis in HuH-7 cells with p53 (show TP53 Proteins) mutation.
TIGAR over-expression could diminish the radiosensitivity of Hs 917.T cells, and the autophagy level induced by ionizing radiation (IR) was also decreased by TIGAR transfection.
The Cdk5 (show CDK5 Proteins)-AMT (show AMT Proteins) signal pathway involved in regulation of DDR (show DDR1 Proteins) by TIGAR.
miR (show MLXIP Proteins)-144 targeted TIGAR, inhibited proliferation, enhanced apoptosis, and increased autophagy in A549 and H460 cells
Results revealed that TIGAR inhibits both apoptosis and autophagy.
TIGAR is correlated with maximal standardized uptake value on FDG (show SMUG1 Proteins)-PET and survival in non-small cell lung cancer.
Data show targeting MUC1 (show MUC1 Proteins)-C is synergistic with bortezomib (BTZ (show CASC3 Proteins)) in suppressing p53 (show TP53 Proteins)-inducible regulator of glycolysis and apoptosis (TIGAR)-mediated regulation of reactive oxygen species levels for combining GO-203 with BTZ (show CASC3 Proteins) in BTZ (show CASC3 Proteins) resistance.
The kinetic properties and the structural similarity of the best substrates of TIGAR make it unlikely that TIGAR modulates cellular fructose 2,6-bisphosphate levels directly.
Results suggest that TIGAR expression changes during development and its expression level may be correlated with the vulnerability of neurons to ischemic injury.
Although mouse TIGAR expression is clearly induced in the intestines of mice following DNA-damaging stress of ionizing radiation, that was not dependent on p53 (show TP53 Proteins) or TAp73 (show TP73 Proteins).
TIGAR protein expression in brain is increased following ischemia reperfusion injury.
Therefore, we conclude that TIGAR knockdown-induced radiosensitization of glioma cells may be dependent on the inhibition of TRX1 (show TXN Proteins) nuclear translocation.
TIGAR protects ischemic brain injury and preserves mitochodrial function.
TIGAR has roles in efficient intestinal regeneration and tumorigenesis
p53 (show TP53 Proteins)/TIGAR-mediated inhibition of myocyte mitophagy is responsible for impairment of mitochondrial integrity and subsequent apoptosis.
p53 (show TP53 Proteins) and TIGAR inhibit glycolysis in hypoxic myocytes and that inhibition of glycolysis is closely involved in apoptosis, suggesting that p53 (show TP53 Proteins) and TIGAR are significant mediators of cellular energy homeostasis and cell death under ischemic stress.
This gene is regulated as part of the p53 tumor suppressor pathway and encodes a protein with sequence similarity to the bisphosphate domain of the glycolytic enzyme that degrades fructose-2,6-bisphosphate. The protein functions by blocking glycolysis and directing the pathway into the pentose phosphate shunt. Expression of this protein also protects cells from DNA damaging reactive oxygen species and provides some protection from DNA damage-induced apoptosis. The 12p13.32 region that includes this gene is paralogous to the 11q13.3 region.
TP53-induced glycolysis and apoptosis regulator
, fructose-2,6-bisphosphatase TIGAR
, probable fructose-2,6-bisphosphatase TIGAR
, chromosome 12 open reading frame 5
, fructose-2,6-bisphosphate 2-phosphatase
, transactivated by NS3TP2 protein