Xinα inhibitors are a class of chemical compounds designed to specifically target and inhibit the function of Xinα, a protein that plays a crucial role in the structural integrity and function of intercalated discs in cardiac muscle. Xinα is part of the Xin repeat-containing family of proteins, which are named after the xin gene discovered in cardiac tissues. This protein is primarily involved in the maintenance and regulation of cytoskeletal dynamics, particularly in the heart, where it interacts with actin filaments and other structural proteins to facilitate proper cell adhesion and mechanical stability at intercalated discs, which are vital for coordinated cardiac muscle contraction. By inhibiting Xinα, these compounds disrupt its interactions with the cytoskeletal components, which can affect cellular structure and function.
Chemically, Xinα inhibitors are designed to target specific regions of the protein that are involved in binding actin or other cytoskeletal elements. These inhibitors may work by preventing the protein-protein interactions necessary for Xinα's role in stabilizing the cytoskeleton or by disrupting the formation of complexes at the intercalated discs. The development of Xinα inhibitors involves high-throughput screening, molecular modeling, and structure-activity relationship (SAR) studies to identify compounds with high specificity for Xinα. By inhibiting Xinα, researchers can explore its precise role in the organization of the actin cytoskeleton and its impact on the overall structural and functional integrity of cardiac tissue. These inhibitors are valuable tools for investigating the mechanisms that underlie cytoskeletal regulation, particularly in specialized cells like cardiomyocytes, and for understanding how disruptions in these processes affect cellular mechanics and tissue homeostasis.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Disrupts actin filament formation, potentially affecting XIRP1-related actin dynamics. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Binds to actin monomers, inhibiting actin polymerization which may influence XIRP1 function. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Stabilizes actin filaments, potentially affecting XIRP1-mediated actin cytoskeletal organization. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
Inhibits Rho-associated protein kinase (ROCK), potentially impacting actin cytoskeletal dynamics related to XIRP1. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $91.00 $267.00 | 13 | |
Inhibits myosin light chain kinase, affecting muscle contraction and potentially XIRP1 activity. | ||||||
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $72.00 $265.00 $495.00 $968.00 | ||
Inhibits myosin II ATPase activity, potentially influencing XIRP1's role in muscle tissue. | ||||||
Colchicine | 64-86-8 | sc-203005 sc-203005A sc-203005B sc-203005C sc-203005D sc-203005E | 1 g 5 g 50 g 100 g 500 g 1 kg | $100.00 $321.00 $2289.00 $4484.00 $18207.00 $34749.00 | 3 | |
Disrupts microtubule polymerization, which might indirectly affect XIRP1 function. | ||||||
Taxol | 33069-62-4 | sc-201439D sc-201439 sc-201439A sc-201439E sc-201439B sc-201439C | 1 mg 5 mg 25 mg 100 mg 250 mg 1 g | $41.00 $74.00 $221.00 $247.00 $738.00 $1220.00 | 39 | |
Stabilizes microtubules, potentially influencing cellular dynamics relevant to XIRP1. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
Inhibits formin-mediated actin polymerization, possibly impacting XIRP1 activity. | ||||||
CK 666 | 442633-00-3 | sc-361151 sc-361151A | 10 mg 50 mg | $321.00 $1040.00 | 5 | |
Inhibits Arp2/3 complex-mediated actin polymerization, potentially affecting XIRP1-related actin structures. | ||||||