LUZP2 Inhibitors
Chemical inhibitors of LUZP2 can significantly affect its function by interacting with and altering the actin cytoskeleton and microtubule networks that LUZP2 is associated with. Wortmannin, as a phosphoinositide 3-kinase inhibitor, can lead to impaired actin filament formation, which is a critical aspect of LUZP2's role in cytoskeletal dynamics. This alteration would result in a less dynamic and responsive cytoskeleton. Similarly, Latrunculin A, by binding to actin monomers, prevents their polymerization and thus can disrupt the integrity of the actin cytoskeleton, which is essential for the structural role LUZP2 plays within the actin network. Cytochalasin D, by capping the barbed ends of actin filaments, also leads to inhibited polymerization, affecting LUZP2's function that relies on well-formed actin filaments. ML-7 and Blebbistatin, which inhibit myosin light chain kinase and myosin II ATPase activity respectively, reduce myosin's interaction with actin, thereby potentially hindering LUZP2's interaction with the actin-myosin network. This can affect cell motility and structure, processes in which LUZP2 is integral.
On the other hand, chemical inhibitors like Marimastat, by inhibiting matrix metalloproteinases, can alter the extracellular matrix, which can indirectly affect LUZP2's role in cell motility and structural integrity. Y-27632, as a ROCK kinase inhibitor, can lead to reduced stress fiber formation, thus potentially inhibiting LUZP2's role in maintaining cytoskeletal integrity. In the realm of microtubule dynamics, Paclitaxel, Nocodazole, Colchicine, and Vinblastine can alter the function of LUZP2 by stabilizing or disrupting microtubules. Paclitaxel stabilizes microtubules, preventing their disassembly, whereas Nocodazole and Colchicine inhibit microtubule polymerization, and Vinblastine binds to tubulin to inhibit microtubule formation. These changes can inhibit LUZP2 by disrupting the dynamic balance required for its function in cellular processes. Jasplakinolide, unlike the others, stabilizes actin filaments, but still can inhibit LUZP2 by hindering the necessary dynamic disassembly of these filaments. By stabilizing or destabilizing these crucial cytoskeletal components, each of these chemicals can inhibit the function of LUZP2, which is reliant on the finely tuned balance of cytoskeletal dynamics.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Wortmannin | 19545-26-7 | sc-3505 sc-3505A sc-3505B | 1 mg 5 mg 20 mg | $66.00 $219.00 $417.00 | 97 | |
Wortmannin is a potent inhibitor of phosphoinositide 3-kinases (PI3K), which are involved in actin cytoskeleton remodeling processes that LUZP2 is thought to participate in. Inhibition of PI3K can lead to impaired actin filament formation and function, thereby inhibiting LUZP2's role in actin cytoskeleton dynamics. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $260.00 $799.00 | 36 | |
Latrunculin A binds to actin monomers and prevents their polymerization, disrupting the dynamics of the actin cytoskeleton. As LUZP2 is associated with actin filaments, the chemical's action can inhibit the structural role LUZP2 plays within the actin network. | ||||||
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 ends of the filaments, which can inhibit LUZP2 if it relies on the proper formation and maintenance of the actin cytoskeleton for its function. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $89.00 $262.00 | 13 | |
ML-7 is an inhibitor of myosin light chain kinase (MLCK), which is crucial for myosin-actin interaction. By inhibiting MLCK, ML-7 can reduce myosin's activity and thus potentially inhibit LUZP2's interaction with the actin-myosin network. | ||||||
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $71.00 $260.00 $485.00 $949.00 | ||
Blebbistatin specifically inhibits myosin II ATPase activity, leading to a reduction in myosin-driven actin filament sliding. As LUZP2 is associated with the actin cytoskeleton, inhibition of myosin II can hinder the mechanical processes where LUZP2 functions. | ||||||
Marimastat | 154039-60-8 | sc-202223 sc-202223A sc-202223B sc-202223C sc-202223E | 5 mg 10 mg 25 mg 50 mg 400 mg | $165.00 $214.00 $396.00 $617.00 $4804.00 | 19 | |
Marimastat is a broad-spectrum inhibitor of matrix metalloproteinases (MMPs), which are involved in extracellular matrix remodeling. Since LUZP2 is implicated in cell motility and structure, inhibiting MMPs can alter the extracellular environment LUZP2 interacts with, indirectly inhibiting its function. | ||||||
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 kinases, which regulate actin cytoskeleton dynamics. Inhibition of ROCK can lead to reduced stress fiber formation and potentially inhibit LUZP2's role in maintaining cytoskeletal integrity. | ||||||
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 | $40.00 $73.00 $217.00 $242.00 $724.00 $1196.00 | 39 | |
Paclitaxel stabilizes microtubules and prevents their disassembly, which can inhibit LUZP2 by disrupting the dynamic instability required for its function in cellular processes such as mitosis and intracellular trafficking. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $58.00 $83.00 $140.00 $242.00 | 38 | |
Nocodazole disrupts microtubule polymers and can inhibit LUZP2 by altering microtubule dynamics, which is essential for processes in which LUZP2 is known to be involved, such as cell division and intracellular transport. | ||||||
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 | $98.00 $315.00 $2244.00 $4396.00 $17850.00 $34068.00 | 3 | |
Colchicine binds to tubulin and inhibits its polymerization into microtubules, thereby potentially inhibiting LUZP2's function if it relies on microtubule-based transport or cell shape maintenance. | ||||||