Date published: 2026-5-16

1-800-457-3801

SCBT Portrait Logo
Seach Input

ZFYVE28 Inhibitors

ZFYVE28 inhibitors belong to a class of chemical compounds that specifically target the zinc finger FYVE domain-containing protein 28 (ZFYVE28). The FYVE domain is a conserved motif found in various proteins involved in membrane trafficking and signaling processes within cells. ZFYVE28, also known as endofin, is one such protein that contains the FYVE domain, playing a crucial role in intracellular membrane dynamics. The inhibition of ZFYVE28 by these specialized compounds disrupts its normal cellular functions, leading to alterations in membrane-related processes.

The primary mechanism of action of ZFYVE28 inhibitors involves interference with the protein's ability to interact with membranes. ZFYVE28 is known to bind to phosphatidylinositol 3-phosphate (PI3P), a phospholipid present in cellular membranes. This interaction is vital for the proper localization and functioning of ZFYVE28 in membrane-associated events. By inhibiting this interaction, ZFYVE28 inhibitors disrupt the normal membrane-related functions mediated by ZFYVE28. This interference may have implications for various cellular processes, including endosomal trafficking, autophagy, and signaling cascades. As research in this field advances, a deeper understanding of the specific effects and potential applications of ZFYVE28 inhibitors in various cellular contexts is likely to emerge.

SEE ALSO...

Items 11 to 12 of 12 total

Display:

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

GW4869

6823-69-4sc-218578
sc-218578A
5 mg
25 mg
$203.00
$611.00
24
(3)

An inhibitor of neutral sphingomyelinase, impacting ceramide production. This could affect membrane dynamics and indirectly inhibit ZFYVE28 if it interacts with ceramide-enriched domains.

YM201636

371942-69-7sc-204193
5 mg
$217.00
6
(1)

An inhibitor of PIKfyve, which is involved in phosphoinositide phosphorylation. By inhibiting PIKfyve, YM201636 could indirectly affect the function of ZFYVE28 in phosphoinositide-mediated processes.