MW 421.6 Da, Purity >95%. Actin polymerization inhibitor. Potent antiproliferative agent. Stabilizes monomeric G-actin. Shows greater potency than Latrunculin B (ab144291). Binds actin monomers near the nucleotide binding cleft with 1:1 stoichiometry. Inhibits growth of cancer cell lines (IC50 values are 142, 142, 142, 166 and 95 nM for A549, H522-T1, HT-29, U-937 and MDA-MB-43 cells respectively). Shows convulsant effects in vivo. .
ARNT-interacting protein, Basic-helix-loop-helix-PAS protein MOP1, Basic-helix-loop-helix-PAS protein MOP2, Class E basic helix-loop-helix protein 73, Class E basic helix-loop-helix protein 78, ECYT4, EPAS1_HUMAN, Endothelial PAS domain-containing protein 1, Endothelial pas domain protein 1, HIF-1, HIF-1-alpha, HIF-1-alpha-like factor, HIF-2-alpha, HIF-alpha, HIF1A_HUMAN, HIF2A, Hypoxia inducible factor 1 alpha isoform I.3, Hypoxia inducible factor 1 alpha subunit, Hypoxia inducible factor 1 alpha subunit basic helix loop helix transcription factor, Hypoxia inducible factor 1, alpha subunit (basic helix loop helix transcription factor), Hypoxia inducible factor 2 alpha subunit, Hypoxia-inducible factor 1-alpha, Hypoxia-inducible factor 2-alpha, MOP 1, MOP 2, Member of PAS protein 1, Member of PAS protein 2, Member of PAS superfamily 1, Member of pas superfamily 2, Member of the PAS Superfamily 1, PAS domain-containing protein 2, PAS domain-containing protein 8, PASD 8, PASD2, bHLHe73, bHLHe78, hifla
MW 421.6 Da, Purity >95%. Actin polymerization inhibitor. Potent antiproliferative agent. Stabilizes monomeric G-actin. Shows greater potency than Latrunculin B (ab144291). Binds actin monomers near the nucleotide binding cleft with 1:1 stoichiometry. Inhibits growth of cancer cell lines (IC50 values are 142, 142, 142, 166 and 95 nM for A549, H522-T1, HT-29, U-937 and MDA-MB-43 cells respectively). Shows convulsant effects in vivo. .
Soluble in ethanol to 10 mM.
Soluble in DMSO to 10 mM.
Actin polymerization inhibitor. Potent antiproliferative agent. Stabilizes monomeric G-actin. Shows greater potency than Latrunculin B (ab144291). Binds actin monomers near the nucleotide binding cleft with 1:1 stoichiometry. Inhibits growth of cancer cell lines (IC50 values are 142, 142, 142, 166 and 95 nM for A549, H522-T1, HT-29, U-937 and MDA-MB-43 cells respectively). Shows convulsant effects in vivo.
HIF-2-alpha and HIF-1 alpha also known as EPAS1 and HIF1A respectively are subunits of the hypoxia-inducible factors which play major roles in response to low oxygen conditions. They form heterodimeric complexes with the ARNT (aryl hydrocarbon receptor nuclear translocator) to function as transcription factors. HIF-1 alpha has a molecular weight of approximately 120 kDa while HIF-2-alpha's weight is around 118 kDa. Both are mostly expressed in various tissues that are sensitive to oxygen levels including but not limited to the kidney liver and heart.
HIF-1 alpha and HIF-2-alpha regulate the transcription of genes involved in angiogenesis metabolism and erythropoiesis among others. When oxygen levels drop these factors stabilise and activate to initiate gene expression changes. They are members of the HIF family and form complexes with ARNT. This functional arrangement serves as a vital response mechanism to hypoxic stress influencing numerous cellular processes and adapting the cell metabolism to changing oxygen availability.
HIF-1 alpha and HIF-2-alpha are central to the hypoxia signaling pathway directly affecting genes like VEGF that stimulate blood vessel formation. They interact with proteins such as PHD (prolyl hydroxylase domain proteins) and VHL (von Hippel-Lindau protein) for regulation. These pathways play roles in the cellular adaptation to low oxygen impacting processes such as glucose metabolism and cell survival. They connect with other pathways too like the mTOR pathway influencing protein synthesis and cellular energy use.
HIF-1 alpha and HIF-2-alpha have associations with cancer and chronic kidney disease. Their unregulated activation is often observed in various cancers promoting an environment that supports tumor growth and survival under hypoxic conditions. In cancers these proteins work closely with VEGF which contributes to angiogenesis and tumor progression. In chronic kidney disease aberrant expression of HIF-1 alpha may influence disease progression by affecting erythropoiesis and iron metabolism linked with proteins like EPO (erythropoietin).
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2D chemical structure image of ab144290, Latrunculin A (LAT-A), Actin polymerization inhibitor
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