Espin inhibitors belong to a specialized class of chemical compounds designed to modulate cellular processes by targeting a specific family of actin-binding proteins known as Espins. Espins are actin-bundling proteins crucial for the proper formation and maintenance of actin-rich structures, particularly in sensory hair cells found in the inner ear. These structures, known as stereocilia, play a fundamental role in mechanotransduction, the process by which mechanical stimuli are converted into electrical signals. Disruptions in stereocilia organization and function can lead to various auditory and vestibular disorders, making Espins and their inhibitors of significant interest in the field of sensory biology.
The chemical structure of Espin inhibitors is meticulously designed to interfere with the binding affinity between Espins and actin filaments, thereby disrupting the formation of stable actin bundles. By selectively targeting Espins, these inhibitors have the potential to unravel the intricate cytoskeletal architecture within sensory hair cells, offering a valuable tool for researchers studying the molecular mechanisms underlying hearing and balance. The development of Espin inhibitors represents a promising avenue for unraveling the complexities of actin dynamics within sensory cells, shedding light on the underlying cellular processes that contribute to normal auditory and vestibular function. The intricate interplay between Espin inhibitors and their molecular targets provides a nuanced understanding of the regulation of actin cytoskeleton dynamics in specialized cellular structures, paving the way for further insights into sensory cell biology.
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
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Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $260.00 $799.00 | 36 | |
Latrunculin A is a toxin that binds to G-actin monomers and prevents their polymerization into F-actin, thus indirectly affecting Espin's actin-bundling activity. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $145.00 $442.00 | 64 | |
Cytochalasin D inhibits actin polymerization by capping the barbed end of the growing actin filament. This can affect Espin's role in maintaining actin filament structures. | ||||||
Swinholide A, Theonella swinhoei | 95927-67-6 | sc-205914 | 10 µg | $135.00 | ||
Swinholide A severs actin filaments, which can impair the stability of structures that Espin helps to maintain. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $180.00 $299.00 | 59 | |
Jasplakinolide stabilizes actin filaments and prevents their depolymerization, which can indirectly influence Espin's actin-bundling activity. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $182.00 $693.00 | 88 | |
Y-27632 is a selective inhibitor of ROCK (Rho-associated coiled-coil kinase), a kinase involved in actin cytoskeleton regulation. Inhibiting ROCK can indirectly affect Espin-mediated actin bundling. | ||||||
(±)-Blebbistatin | 674289-55-5 | sc-203532B sc-203532 sc-203532A sc-203532C sc-203532D | 5 mg 10 mg 25 mg 50 mg 100 mg | $179.00 $307.00 $455.00 $924.00 $1689.00 | 7 | |
Blebbistatin inhibits myosin II, thereby affecting actin-myosin interaction. This can indirectly affect the structural stability of actin structures where Espin is active. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $89.00 $262.00 | 13 | |
ML-7 inhibits myosin light chain kinase (MLCK), which plays a role in actin-myosin interaction. Inhibiting MLCK can indirectly affect Espin's role in actin structure maintenance. | ||||||
Wiskostatin | 253449-04-6 | sc-204399 sc-204399A sc-204399B sc-204399C | 1 mg 5 mg 25 mg 50 mg | $48.00 $122.00 $432.00 $812.00 | 4 | |
Wiskostatin inhibits the N-WASP-Arp2/3 pathway, which is involved in actin polymerization. This can indirectly affect Espin's function in actin-bundling. | ||||||
CK 666 | 442633-00-3 | sc-361151 sc-361151A | 10 mg 50 mg | $315.00 $1020.00 | 5 | |
CK-666 inhibits the Arp2/3 complex, a key player in the branching of actin filaments. This can indirectly impact Espin's role in actin structure maintenance. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2 inhibits formins, which are involved in unbranched actin filament formation. This can indirectly affect the function of Espin. |