Date published: 2026-2-14

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VPS45 Activators

VPS45 activators belong to a chemical class engineered to interact with and modulate the activity of the VPS45 protein. VPS45, also known as Vacuolar Protein Sorting 45, is an essential component of the endosomal sorting complexes required for transport (ESCRT) machinery. This machinery is involved in sorting and trafficking proteins within the endosomal pathway, directing them to their appropriate destinations within the cell. VPS45 specifically plays a critical role in membrane fusion events during endosomal trafficking, facilitating the formation of multivesicular bodies (MVBs) and the sorting of cargo proteins into intraluminal vesicles for degradation or recycling. Additionally, VPS45 is implicated in the regulation of membrane dynamics and organelle morphology, further underscoring its significance in cellular processes.

Research into VPS45 activators focuses on elucidating the molecular mechanisms underlying their interaction with the VPS45 protein and understanding how this interaction modulates endosomal trafficking and membrane dynamics. By targeting VPS45 activity, these activators have the potential to influence the efficiency and specificity of protein sorting within the endosomal pathway, thereby impacting cellular homeostasis and function. Understanding the pharmacological properties of VPS45 activators is crucial for deciphering how they affect VPS45-mediated processes and potentially alter cellular physiology. By delving into the biological functions and regulatory mechanisms of VPS45, researchers aim to deepen our understanding of intracellular trafficking and organelle dynamics and may uncover novel insights into the molecular pathways governing cellular organization. Continued exploration of VPS45 activators holds promise for advancing our knowledge of cellular biology and may provide insights into new strategies for manipulating cellular function within experimental contexts.

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Lithium

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88
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Wortmannin

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97
(3)

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SB 203580

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284
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