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Suggest that CTMP may therefore play a critical role in mitochondrial-mediated apoptosis in lung cancer cells.
Data show low or moderate methylation was found in seven selected genes BAD, BBC3 (zeige BBC3 ELISA Kits), CAV1 (zeige CAV1 ELISA Kits), CDK2AP1 (zeige CDK2AP1 ELISA Kits), NPM1 (zeige NPM1 ELISA Kits), PRKCDBP (zeige PRKCDBP ELISA Kits) and THEM4.
CTMP induces translocation of Akt (zeige AKT1 ELISA Kits) to the membrane and thereby increases the level of Akt (zeige AKT1 ELISA Kits) phosphorylation. As a result, CTMP enhances various cellular activities that are principally mediated by the PI3-kinase (zeige PIK3CA ELISA Kits)/Akt (zeige AKT1 ELISA Kits) pathway.
Proper maturation of CTMP is essential for its pro-apoptotic function. CTMP delays PKB (zeige AKT1 ELISA Kits) phosphorylation following cell death induction, suggesting that CTMP regulates apoptosis via inhibition of PKB (zeige AKT1 ELISA Kits).
Phosphorylation on Ser37/Ser38 of CTMP is important for the prevention of mitochondrial localization of CTMP, eventually leading to cell death by binding to heat shock protein 70 (zeige HSP70 ELISA Kits).
Results suggest that Akt (zeige AKT1 ELISA Kits) is phosphorylated and translocated to nucleus after traumatic brain injury (TBI) to exert neuroprotective effects; however, CTMP is simultaneously triggered to inhibit the phosphorylation of Akt (zeige AKT1 ELISA Kits)
Protein kinase B (PKB) is a major downstream target of receptor tyrosine kinases that signal via phosphatidylinositol 3-kinase. Upon cell stimulation, PKB is translocated to the plasma membrane, where it is phosphorylated in the C-terminal regulatory domain. The protein encoded by this gene negatively regulates PKB activity by inhibiting phosphorylation. Transcription of this gene is commonly downregulated in glioblastomas.
thioesterase superfamily member 4
, acyl-coenzyme A thioesterase THEM4
, C-terminal modulator protein
, acyl-CoA thioesterase THEM4
, carboxyl-terminal modulator protein