Tyk Inhibitors
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
JAK Inhibitor I | 457081-03-7 | sc-204021 sc-204021A | 500 µg 1 mg | $156.00 $339.00 | 59 | |
JAK Inhibitor I acts as a selective modulator of the Janus kinase (JAK) family, exhibiting unique binding affinities that disrupt the phosphorylation of target proteins. Its molecular interactions are characterized by specific hydrogen bonding and hydrophobic contacts, which stabilize the inhibitor-receptor complex. The compound's kinetic profile indicates a competitive inhibition mechanism, effectively altering signal transduction pathways while maintaining a high degree of specificity for JAK isoforms. | ||||||
Lavendustin C | 125697-93-0 | sc-202207 sc-202207B sc-202207A sc-202207C | 1 mg 5 mg 10 mg 50 mg | $86.00 $188.00 $333.00 $1457.00 | ||
Lavendustin C functions as a potent Tyk inhibitor, showcasing a distinctive ability to interfere with tyrosine kinase activity through specific allosteric modulation. Its interactions involve intricate electrostatic and van der Waals forces, which enhance binding affinity and selectivity. The compound exhibits unique reaction kinetics, characterized by a rapid onset of inhibition, allowing for precise regulation of downstream signaling pathways. Its structural features contribute to a favorable conformational adaptability, optimizing its inhibitory effects. | ||||||
Ageladine A, TFA | 643020-13-7 | sc-396549 | 200 µg | $364.00 | ||
Ageladine A, TFA acts as a selective Tyk inhibitor, demonstrating a unique capacity to disrupt tyrosine kinase signaling through competitive binding at the active site. Its molecular structure facilitates strong hydrogen bonding and hydrophobic interactions, enhancing specificity. The compound exhibits a distinctive kinetic profile, with a delayed onset of inhibition that allows for nuanced modulation of cellular responses. Additionally, its conformational flexibility supports diverse interaction dynamics within the kinase domain. | ||||||
Caffeic Acid | 331-39-5 | sc-200499 sc-200499A | 1 g 5 g | $32.00 $62.00 | 1 | |
Caffeic Acid functions as a Tyk inhibitor by engaging in non-covalent interactions that stabilize its binding to the enzyme's active site. Its unique phenolic structure promotes electron delocalization, enhancing its reactivity and affinity for tyrosine residues. The compound's ability to form π-π stacking interactions contributes to its selectivity, while its dynamic conformational changes facilitate adaptability in various biochemical environments, influencing downstream signaling pathways. | ||||||
N-(2-Chloro-6-methylphenyl)-2-[(6-chloro-2-methyl-4-pyrimidinyl)amino]-5-thiazolecarboxamide | 302964-08-5 | sc-207904 sc-207904A sc-207904B sc-207904C sc-207904D | 250 mg 500 mg 1 g 10 g 100 g | $178.00 $260.00 $420.00 $940.00 $1800.00 | ||
N-(2-Chloro-6-methylphenyl)-2-[(6-chloro-2-methyl-4-pyrimidinyl)amino]-5-thiazolecarboxamide exhibits potent Tyk inhibition through specific hydrogen bonding and hydrophobic interactions with the enzyme's active site. Its thiazole moiety enhances molecular rigidity, promoting effective spatial orientation for optimal binding. The compound's unique substitution patterns allow for selective interactions, influencing reaction kinetics and modulating enzymatic activity in complex biochemical systems. | ||||||
TCS 21311 | 1260181-14-3 | sc-362804 sc-362804A | 10 mg 50 mg | $270.00 $1077.00 | ||
TCS 21311 functions as a Tyk inhibitor by engaging in precise electrostatic interactions and forming stable complexes with the enzyme's active site. The presence of a thiazole ring contributes to its conformational stability, facilitating enhanced binding affinity. Additionally, the compound's unique halogen substitutions create a distinctive electronic environment, which influences the rate of reaction and alters the enzyme's catalytic efficiency, thereby impacting downstream signaling pathways. | ||||||
ψ-Tectorigenin | 13111-57-4 | sc-296865 | 250 µg | $400.00 | ||
ψ-Tectorigenin acts as a Tyk inhibitor through its ability to form transient hydrogen bonds and hydrophobic interactions with key residues in the enzyme's active site. Its unique structural features, including a fused aromatic system, enhance its conformational adaptability, allowing for optimal fit during binding. The compound's specific steric hindrance modifies the enzyme's kinetics, leading to altered substrate accessibility and modulation of associated signaling cascades. | ||||||
Adaphostin | 241127-58-2 | sc-291833 sc-291833A | 10 mg 50 mg | $129.00 $560.00 | ||
Adaphostin functions as a Tyk inhibitor by engaging in specific electrostatic interactions with charged amino acids within the enzyme's active site. Its unique structural motifs, including a rigid scaffold, facilitate precise orientation during binding, enhancing selectivity. The compound's ability to disrupt critical protein-protein interactions alters the conformational dynamics of Tyk, ultimately influencing downstream signaling pathways and cellular responses. | ||||||