Latrunculin A (LAT-A), Actin polymerization inhibitor
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(29 Publications)
Latrunculin A (LAT-A) is an actin polymerization inhibitor. Stabilizes monomeric G-actin and disrupts F-actin organization. Shows greater potency than Latrunculin B (ab144291). MW 421.6
- 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)
- Potent antiproliferative agent
- Available in different sizes to fit your experimental needs
View Alternative Names
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
- Chemical Structure
Lab
Chemical Structure - Latrunculin A (LAT-A), Actin polymerization inhibitor (AB144290)
2D chemical structure image of ab144290, Latrunculin A (LAT-A), Actin polymerization inhibitor
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Pathways
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.
Biological function summary
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.
Publications (29)
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Journal of virology 99:e0211324 PubMed39907281
2025
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Cell death and differentiation 32:546-560 PubMed39511403
2024
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Journal of virology 98:e0060624 PubMed38809020
2024
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Nature communications 15:541 PubMed38225245
2024
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Current biology : CB 34:245-259.e8 PubMed38096821
2023
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Biophysical journal 122:767-783 PubMed36739478
2023
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Advanced healthcare materials 12:e2201720 PubMed36447307
2022
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eLife 11: PubMed36111670
2022
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Cancer research communications 2:914-928 PubMed36922934
2022
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The Journal of cell biology 221: PubMed35575797
2022
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