Date published: 2026-5-29

1-800-457-3801

SCBT Portrait Logo
Seach Input

StARD13 Inhibitors

StARD13 inhibitors represent a chemically diverse class of compounds engineered to exert selective control over the functional activity of the StAR-related lipid transfer domain-containing 13 (StARD13) protein, also known as DLC2. StARD13 is a multifunctional protein that is intricately involved in vital cellular processes, including actin cytoskeleton organization and lipid metabolism regulation. These inhibitors are meticulously designed to interact with specific binding sites or structural domains within the StARD13 protein, leading to altered molecular interactions and subsequent modulation of cellular pathways.

The chemical structures of StARD13 inhibitors can vary widely, encompassing a spectrum of small molecules with unique arrangements that ensure optimal binding and specificity for StARD13. These compounds are strategically designed to mitigate any off-target effects, thereby honing their impact solely on the intended biological processes. A prominent mode of action employed by StARD13 inhibitors involves disrupting the interaction between StARD13 and the actin cytoskeleton. By binding to specific regions of the protein, these inhibitors interfere with its ability to regulate actin dynamics, which, in turn, influences essential cellular functions such as cell migration, adhesion, and morphological changes.

Moreover, StARD13 inhibitors can also impede lipid metabolism by targeting StARD13's lipid transfer domain. This domain is a hallmark feature of the StARD protein family and plays a central role in facilitating the transfer of lipids between cellular membranes. Inhibitors designed to interact with this domain have the ability to disrupt the proper movement of lipids, leading to a cascade of effects on downstream cellular pathways that rely on accurate lipid distribution. The precision engineering behind StARD13 inhibitors allows for the controlled manipulation of StARD13's intricate molecular interactions and functions, opening avenues for extensive investigation into the broader biological implications of its activity. In conclusion, StARD13 inhibitors represent a fascinating class of compounds with diverse chemical structures, each tailored to modulate StARD13's engagement in critical cellular processes. Through targeted disruption of StARD13's interactions with the actin cytoskeleton and lipid transfer domain, these inhibitors provide valuable tools for dissecting the intricate web of pathways that StARD13 governs. While their applications extend beyond the scope of this description, StARD13 inhibitors hold substantial promise for advancing our understanding of cellular biology and uncovering novel avenues for interventions.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

SMIFH2

340316-62-3sc-507273
5 mg
$140.00
(0)

SMIFH2 is a small molecule inhibitor that disrupts the binding of STARD13 to the actin cytoskeleton, affecting cell migration and potentially having implications in cancer metastasis.

Latrunculin A, Latrunculia magnifica

76343-93-6sc-202691
sc-202691B
100 µg
500 µg
$265.00
$815.00
36
(2)

While primarily known as an actin polymerization inhibitor, Latrunculin A indirectly affects STARD13 by disrupting actin dynamics and, subsequently, the interactions of STARD13 with the cytoskeleton.

Artemisinin

63968-64-9sc-202960
sc-202960A
100 mg
1 g
$45.00
$252.00
1
(1)

Artemisinin is a natural compound with anti-malarial properties that can indirectly impact STARD13 by affecting its interactions with other proteins involved in actin regulation.

Thapsigargin

67526-95-8sc-24017
sc-24017A
1 mg
5 mg
$136.00
$446.00
114
(2)

Thapsigargin is a compound that can modulate STARD13 by affecting calcium signaling, which could influence its function in lipid transfer and actin regulation.

Cytochalasin D

22144-77-0sc-201442
sc-201442A
1 mg
5 mg
$165.00
$486.00
64
(4)

Similar to Latrunculin A, Cytochalasin D is an actin inhibitor that indirectly affects STARD13 through its impact on the cytoskeleton.