SEE ALSO...
Items 11 to 14 of 14 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
ZM-306416 | 690206-97-4 | sc-200676 sc-200676A | 1 mg 10 mg | $75.00 $152.00 | ||
ZM-306416 functions as a selective Src inhibitor, characterized by its ability to form stable complexes with the Src kinase domain. This compound engages in non-covalent interactions that enhance its binding affinity, effectively modulating the enzyme's conformational dynamics. The unique steric properties of ZM-306416 allow it to selectively disrupt key protein-protein interactions, thereby altering downstream signaling pathways. Its kinetic behavior indicates a prolonged inhibitory effect, contributing to sustained modulation of Src activity. | ||||||
PP121 | 1092788-83-4 | sc-301605 | 5 mg | $139.00 | 1 | |
PP121 acts as a selective Src inhibitor, distinguished by its unique ability to interact with the Src kinase's active site through specific hydrogen bonding and hydrophobic interactions. This compound exhibits a remarkable selectivity profile, allowing it to preferentially inhibit Src over other kinases. Its rapid kinetics facilitate a swift onset of action, while its structural conformation promotes effective disruption of critical signaling cascades, ultimately influencing cellular responses. | ||||||
Src/EGFR inhibitor | 131023-24-0 | sc-3050 | 0.5 mg | $95.00 | 2 | |
Src/EGFR Inhibitor is characterized by its dual-targeting mechanism, engaging both Src and EGFR pathways through intricate molecular interactions. The compound's unique binding affinity is attributed to its ability to form stable complexes with key residues in the kinase domains, leading to conformational changes that hinder enzymatic activity. Its kinetic profile reveals a fast association rate, enabling efficient modulation of downstream signaling networks, thereby altering cellular dynamics significantly. | ||||||
Dasatinib β-D-Glucuronide | sc-218082 | 1 mg | $430.00 | |||
Dasatinib β-D-Glucuronide exhibits a distinctive interaction profile with Src kinases, characterized by selective binding to the ATP-binding pocket. This interaction induces a conformational shift that stabilizes the inactive form of the enzyme, effectively disrupting its catalytic function. The compound's solubility and stability in physiological conditions enhance its bioavailability, while its metabolic pathways suggest a unique role in modulating cellular signaling cascades, influencing various biological processes. | ||||||