Eg5 Inhibitors
Items 1 to 10 of 14 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Gossypol | 303-45-7 | sc-200501 sc-200501A | 25 mg 100 mg | $114.00 $225.00 | 12 | |
Gossypol, functioning as an Eg5, exhibits intriguing characteristics as an acid halide, particularly through its ability to form covalent bonds with thiol groups, which can significantly alter protein interactions. Its planar structure allows for effective π-π stacking with aromatic residues, enhancing binding affinity. Additionally, Gossypol's hydrophobic regions contribute to its selective partitioning in lipid environments, influencing its reactivity and interaction dynamics in biological systems. | ||||||
Monastrol | 254753-54-3 | sc-202710 sc-202710A | 1 mg 5 mg | $120.00 $233.00 | 10 | |
Monastrol, as an Eg5 inhibitor, showcases unique properties as an acid halide, particularly through its selective interaction with the motor protein's ATP-binding site. Its rigid bicyclic structure facilitates specific hydrogen bonding and steric hindrance, disrupting microtubule dynamics. The compound's hydrophilic and hydrophobic balance enhances solubility in various environments, influencing its kinetic behavior and interaction with cellular components, ultimately affecting mitotic processes. | ||||||
Chlorpromazine, Hydrochloride | 69-09-0 | sc-202537 sc-202537A sc-202537B sc-202537C sc-202537D | 500 mg 5 g 25 g 100 g 250 g | $39.00 $55.00 $149.00 $496.00 $1087.00 | 7 | |
Chlorpromazine, Hydrochloride, as an Eg5 inhibitor, exhibits distinctive characteristics as an acid halide, particularly through its ability to form stable complexes with target proteins. Its planar tricyclic structure allows for effective π-π stacking interactions, enhancing binding affinity. The compound's amphipathic nature promotes diverse solubility profiles, influencing its diffusion rates and reaction kinetics within cellular environments, thereby impacting microtubule organization and cellular dynamics. | ||||||
Eg5 Inhibitor V, trans-24 | 869304-55-2 | sc-202596 | 1 mg | $93.00 | ||
Eg5 Inhibitor V, trans-24, functions as an Eg5 inhibitor by engaging in specific hydrogen bonding interactions with the motor protein, disrupting its function. Its unique stereochemistry facilitates selective binding, altering the conformational dynamics of the target. The compound's lipophilic characteristics enhance membrane permeability, while its ability to modulate microtubule dynamics contributes to its distinct biochemical behavior, influencing cellular processes at a molecular level. | ||||||
SB 743921 | 940929-33-9 | sc-364609 sc-364609A | 5 mg 10 mg | $260.00 $653.00 | ||
SB 743921 acts as an Eg5 inhibitor through its unique ability to interfere with the ATPase activity of the kinesin motor protein. This compound exhibits a distinctive binding affinity, allowing it to stabilize specific conformations of Eg5, thereby impeding its motility along microtubules. Additionally, its structural features promote effective interactions with the protein's active site, leading to altered reaction kinetics and a profound impact on mitotic spindle assembly. | ||||||
Eg5 Inhibitor VII | 912953-25-4 | sc-221578 | 5 mg | $153.00 | 1 | |
Eg5 Inhibitor VII functions as a selective inhibitor of the Eg5 kinesin motor protein, characterized by its ability to disrupt microtubule dynamics. This compound engages in specific molecular interactions that alter the conformational landscape of Eg5, effectively hindering its function in mitotic processes. Its unique structural attributes facilitate targeted binding, resulting in modified kinetic profiles that significantly affect cellular transport mechanisms and spindle organization. | ||||||
Eg5 Inhibitor VI | sc-281686 | 5 mg | $398.00 | |||
Eg5 Inhibitor VI acts as a potent disruptor of the Eg5 kinesin motor protein, showcasing a unique binding affinity that alters the protein's structural integrity. This compound interacts with key residues within the motor domain, leading to a conformational shift that impairs ATPase activity. The inhibitor's distinct molecular architecture enhances its selectivity, resulting in pronounced effects on microtubule organization and cellular motility, ultimately influencing mitotic spindle dynamics. | ||||||
S-Trityl-L-cysteine | 2799-07-7 | sc-202799 sc-202799A | 1 g 5 g | $31.00 $65.00 | 6 | |
S-Trityl-L-cysteine serves as a selective modulator of the Eg5 kinesin motor protein, exhibiting a unique mechanism of action through its interaction with specific amino acid residues. This compound stabilizes a non-productive conformation of Eg5, effectively hindering its motor function. The steric bulk of the trityl group contributes to its specificity, disrupting microtubule dynamics and influencing cellular transport pathways, thereby impacting mitotic processes. | ||||||
K 858 | 72926-24-0 | sc-300856 sc-300856A | 10 mg 50 mg | $159.00 $693.00 | ||
K 858 acts as a potent inhibitor of the Eg5 kinesin motor protein, characterized by its ability to bind selectively to the motor domain. This compound alters the conformational dynamics of Eg5, promoting a state that impedes ATP hydrolysis and motor activity. Its unique structural features enhance binding affinity, leading to a significant reduction in microtubule sliding. Consequently, K 858 disrupts mitotic spindle assembly, affecting cellular division processes. | ||||||
trans-HR22C16 | 462630-41-7 | sc-202842 | 1 mg | $128.00 | ||
trans-HR22C16 functions as a selective inhibitor of the Eg5 kinesin motor protein, exhibiting unique interactions with the ATP-binding site. Its distinct molecular architecture facilitates strong binding, which stabilizes a conformation that hinders the motor's ability to translocate along microtubules. This compound's kinetic profile reveals a slow dissociation rate, enhancing its efficacy in disrupting the normal dynamics of mitotic spindle formation and cellular transport mechanisms. | ||||||