PI3K/AKT signaling, MAPK/ERK pathway, mTOR signaling, Hedgehog pathway, protein degradation, apoptosis, calcium homeostasis, or protein glycosylation. These compounds are not directly antagonistic to LOC146429 but could modulate the cellular environment or the signaling pathways in which LOC146429 presumably participates. Wortmannin and LY294002 are well-known inhibitors of PI3K, and by inhibiting this kinase, they can affect downstream signaling pathways that are crucial for cell survival, proliferation, and metabolism, which may involve LOC146429. U0126 and PD98059 target the MEK1/2, which are upstream regulators of the ERK pathway, a critical pathway for cell division and differentiation. SB203580 and SP600125 are inhibitors of p38 MAP kinase and JNK, respectively, which are involved in the cellular response to stress and inflammation and might intersect with LOC146429's function.
Rapamycin is a specific inhibitor of mTOR, a central regulator of cell growth, which could influence any processes that LOC146429 is associated with in terms of cell growth control. Cyclopamine targets the Hedgehog signaling pathway, which is influential during development and in the regulation of stem cells, potentially affecting LOC146429's role in these processes. Bortezomib disrupts the proteasome's function, which is essential for protein degradation and turnover, and could, therefore, affect the stability and levels of LOC146429 if it were subject to proteasomal degradation. Z-VAD-FMK is a broad-spectrum caspase inhibitor that can prevent apoptosis, potentially influencing any apoptotic regulation by LOC146429. Thapsigargin disrupts calcium homeostasis by inhibiting SERCA pumps in the endoplasmic reticulum, which can have widespread effects on cellular signaling and function, potentially including the function of LOC146429. Lastly, Tunicamycin inhibits N-linked glycosylation, a post-translational modification that can affect protein folding and stability, and thus could impact thecorrect function and stability of LOC146429 if it undergoes glycosylation.
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