HSP 90 Inhibitors
Items 21 to 26 of 26 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
KW-2478 | 819812-04-9 | sc-364519 sc-364519A | 10 mg 50 mg | $555.00 $1455.00 | ||
KW-2478 is a selective inhibitor of Hsp90 that engages the protein's N-terminal domain, disrupting its ATPase activity. This compound exhibits unique binding dynamics, characterized by a combination of hydrophobic interactions and electrostatic complementarity, which enhances its affinity for the target. The resultant conformational changes in Hsp90 hinder its chaperoning capabilities, affecting client protein maturation and stability. KW-2478's distinct molecular architecture allows for precise modulation of chaperone-mediated pathways, influencing cellular homeostasis. | ||||||
BIIB 021 | 848695-25-0 | sc-364434 sc-364434A | 5 mg 25 mg | $128.00 $650.00 | ||
BIIB 021 acts as a selective inhibitor of Hsp90, engaging its N-terminal domain to disrupt ATPase activity. This compound uniquely stabilizes the Hsp90-client complex, preventing the proper folding and maturation of client proteins. Its interaction profile is characterized by a distinct set of hydrophobic and electrostatic interactions, which modulate the chaperone's conformational dynamics, ultimately influencing cellular stress response pathways and protein homeostasis. | ||||||
AT13387 | 912999-49-6 | sc-364415 sc-364415A | 10 mg 50 mg | $555.00 $1606.00 | ||
AT13387 functions as a potent inhibitor of Hsp90, targeting its N-terminal domain to impede ATP binding and hydrolysis. This compound uniquely alters the chaperone's conformational landscape, leading to the destabilization of client protein complexes. Its specific interactions involve a combination of hydrophobic pockets and hydrogen bonding, which fine-tune the chaperone's activity and affect the regulation of protein folding and degradation pathways within the cell. | ||||||
Novobiocin | 303-81-1 | sc-362034 sc-362034A | 5 mg 25 mg | $128.00 $380.00 | ||
Novobiocin functions as a potent inhibitor of Hsp90 by binding to its N-terminal domain, effectively altering the protein's conformational landscape. This interaction disrupts the ATP-binding site, leading to a decrease in ATP hydrolysis and subsequent chaperone activity. The compound's unique ability to form specific hydrogen bonds and hydrophobic interactions with key residues enhances its inhibitory potency, ultimately affecting the stability and functionality of client proteins within the cellular environment. | ||||||
VER-49009 | 940289-57-6 | sc-357409 sc-357409A sc-357409B sc-357409C | 500 µg 1 mg 5 mg 10 mg | $123.00 $235.00 $992.00 $1725.00 | ||
VER-49009 acts as a selective inhibitor of Hsp90, engaging with its N-terminal domain to disrupt the ATPase cycle. This compound uniquely stabilizes an inactive conformation of Hsp90, preventing the proper folding and maturation of client proteins. Its interactions are characterized by a distinct network of hydrophobic and polar contacts, which modulate the chaperone's structural dynamics and influence the cellular stress response mechanisms. | ||||||
VER-50589 | 747413-08-7 | sc-296692 sc-296692A | 500 µg 1 mg | $70.00 $110.00 | ||
VER-50589 acts as a selective inhibitor of Hsp90, engaging with the protein's N-terminal domain to induce conformational changes. This compound uniquely stabilizes a closed conformation of Hsp90, impeding its ATPase activity and disrupting the chaperone cycle. Its distinct molecular interactions, including π-π stacking and van der Waals forces with critical amino acids, contribute to its efficacy in modulating protein folding and stability within the cellular milieu. | ||||||