BAIAP2L2 Inhibitors
Chemical inhibitors of BAIAP2L2 disrupt the normal function of this protein by targeting various pathways and molecules involved in actin cytoskeleton organization. LY294002 and Wortmannin are two such inhibitors that achieve this by targeting phosphoinositide 3-kinases (PI3K), essential components upstream of the PI3K/Akt signaling pathway that BAIAP2L2 is part of. The inhibition of PI3K by these compounds leads to a decrease in Akt activity, which is a key regulator of several proteins that participate in cytoskeletal changes, including those involving BAIAP2L2. Another inhibitor, Y-27632, targets the Rho-associated protein kinase (ROCK), a significant player in actin cytoskeleton organization. By inhibiting ROCK, Y-27632 disrupts downstream signaling that might involve BAIAP2L2, leading to its functional inhibition. Similarly, NSC 23766 prevents the activation of Rac1 by hindering its interaction with GEFs, thus impeding the actin cytoskeleton organization where BAIAP2L2 is implicated.
Additional inhibitors like CCG-1423, ML141, and CK-636 employ varied mechanisms to disrupt BAIAP2L2 function. CCG-1423 inhibits RhoA-mediated gene transcription, which is significant for actin cytoskeleton organization, thereby indirectly affecting BAIAP2L2's role. ML141 specifically targets Cdc42, a small GTPase, and its inhibition can impede the signaling necessary for BAIAP2L2 to influence actin cytoskeleton dynamics. CK-636, on the other hand, inhibits the Arp2/3 complex, which is vital for actin nucleation and branching, processes that BAIAP2L2 is associated with. SMIFH2 interferes with formin-mediated actin assembly by inhibiting formin homology 2 domains, which could lead to a reduction in BAIAP2L2's ability to reorganize the actin cytoskeleton. Latrunculin A, by binding to actin monomers, prevents their polymerization, and this action can disrupt cellular functions that depend on the actin dynamics BAIAP2L2 is involved with. Blebbistatin and Swinholide A both target actin filaments but in opposite ways; while Blebbistatin inhibits myosin II ATPase activity, affecting actomyosin contractility, Swinholide A severs actin filaments, reducing the amount of filamentous actin. Lastly, Jasplakinolide stabilizes actin filaments, which can also inhibit BAIAP2L2 by preventing the dynamic remodeling of the actin cytoskeleton. Each of these chemicals, by affecting different molecules that interact with or regulate BAIAP2L2, can lead to the functional inhibition of BAIAP2L2's role in actin cytoskeleton dynamics.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
LY 294002 | 154447-36-6 | sc-201426 sc-201426A | 5 mg 25 mg | $123.00 $400.00 | 148 | |
LY294002 inhibits phosphoinositide 3-kinases (PI3K), which are upstream regulators in the PI3K/Akt signaling pathway. BAIAP2L2 is implicated in actin cytoskeleton reorganization. PI3K inhibition can lead to reduced Akt activity, thereby inhibiting actin remodeling activities associated with BAIAP2L2. | ||||||
Wortmannin | 19545-26-7 | sc-3505 sc-3505A sc-3505B | 1 mg 5 mg 20 mg | $67.00 $223.00 $425.00 | 97 | |
Wortmannin is another potent inhibitor of PI3K. By inhibiting PI3K, it prevents the activation of the downstream effector Akt, which is necessary for the full activation of several proteins involved in cytoskeletal changes, potentially inhibiting BAIAP2L2's role in these processes. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
Y-27632 selectively inhibits ROCK (Rho-associated protein kinase), which is involved in actin cytoskeleton organization. By inhibiting ROCK, the chemical can disrupt the downstream signaling that may involve BAIAP2L2, leading to its functional inhibition. | ||||||
NSC 23766 | 733767-34-5 | sc-204823 sc-204823A | 10 mg 50 mg | $151.00 $609.00 | 75 | |
NSC 23766 inhibits Rac1 activation by interfering with the interaction of Rac1 with its specific GEFs, disrupting actin cytoskeleton organization. BAIAP2L2, associated with actin polymerization, can be functionally inhibited by the disruption of Rac1 activity. | ||||||
CCG-1423 | 285986-88-1 | sc-205241 sc-205241A | 1 mg 5 mg | $30.00 $90.00 | 8 | |
CCG-1423 inhibits RhoA-mediated gene transcription, ultimately leading to the inhibition of actin cytoskeleton organization. BAIAP2L2 function is closely linked to actin dynamics; thus, inhibiting RhoA signaling can lead to functional inhibition of BAIAP2L2. | ||||||
ML 141 | 71203-35-5 | sc-362768 sc-362768A | 5 mg 25 mg | $137.00 $512.00 | 7 | |
ML141 specifically inhibits Cdc42, a small GTPase involved in actin filament assembly. As BAIAP2L2 is implicated in cytoskeletal rearrangement, inhibition of Cdc42 can impair the signaling processes necessary for BAIAP2L2 to exert its function on the actin cytoskeleton. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2 is an inhibitor of formin homology 2 domains in formins, which mediate the formation of long actin filaments. Since BAIAP2L2 is involved in actin cytoskeleton reorganization, inhibiting formin-mediated actin assembly can subsequently inhibit BAIAP2L2 function. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A binds to actin monomers and prevents their polymerization. The inhibition of actin polymerization can disrupt the cellular functions where BAIAP2L2 is involved, thereby leading to its functional inhibition by impairing the cytoskeletal dynamics it influences. | ||||||
(±)-Blebbistatin | 674289-55-5 | sc-203532B sc-203532 sc-203532A sc-203532C sc-203532D | 5 mg 10 mg 25 mg 50 mg 100 mg | $183.00 $313.00 $464.00 $942.00 $1723.00 | 7 | |
Blebbistatin is an inhibitor of myosin II ATPase activity. By inhibiting myosin II, it can disrupt the contractile process of actomyosin, which is necessary for cell motility and shape changes that BAIAP2L2 may regulate, thus functionally inhibiting BAIAP2L2. | ||||||
Swinholide A, Theonella swinhoei | 95927-67-6 | sc-205914 | 10 µg | $135.00 | ||
Swinholide A severs actin filaments and decreases the overall amount of filamentous actin in cells. This can lead to the functional inhibition of BAIAP2L2 by drastically altering the actin cytoskeleton that BAIAP2L2 is known to interact with. | ||||||