Items 41 to 50 of 107 total
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
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Berberine hydrochloride | 633-65-8 | sc-204645 sc-204645A sc-204645B sc-204645C sc-204645D | 1 g 5 g 25 g 100 g 500 g | $40.00 $55.00 $130.00 $367.00 $1295.00 | 5 | |
Berberine hydrochloride demonstrates COX-2 inhibition by engaging in hydrogen bonding and hydrophobic interactions with the enzyme's active site. This binding alters the enzyme's conformation, leading to a decrease in its activity. Furthermore, its quaternary ammonium structure enhances solubility in biological systems, facilitating its distribution and interaction with cellular membranes, which may modulate inflammatory signaling cascades at a molecular level. | ||||||
Indomethacin Methyl Ester | 1601-18-9 | sc-207757 | 10 mg | $300.00 | ||
Indomethacin Methyl Ester exhibits selective COX-2 inhibition through its unique ability to form stable π-π stacking interactions with aromatic residues in the enzyme's active site. This interaction not only stabilizes the enzyme-substrate complex but also influences the reaction kinetics by altering the transition state. Additionally, its ester functional group enhances lipophilicity, promoting membrane permeability and facilitating deeper tissue penetration, which may impact local biochemical pathways. | ||||||
N-tert-Butyl-a-phenylnitrone | 3376-24-7 | sc-202722 sc-202722A | 500 mg 1 g | $51.00 $87.00 | ||
N-tert-Butyl-a-phenylnitrone demonstrates selective COX-2 inhibition by engaging in specific hydrogen bonding with key amino acid residues within the enzyme's active site. This interaction modulates the enzyme's conformation, effectively altering its catalytic efficiency. The presence of the nitrone functional group contributes to its unique electron-withdrawing properties, influencing redox reactions and enhancing its stability in biological systems, thereby affecting downstream signaling pathways. | ||||||
Flurbiprofen | 5104-49-4 | sc-202158 sc-202158A | 100 mg 1 g | $69.00 $104.00 | ||
Flurbiprofen exhibits selective COX-2 inhibition through its unique ability to form hydrophobic interactions with the enzyme's active site, stabilizing a specific conformation that reduces its enzymatic activity. The presence of its aromatic structure enhances π-π stacking interactions, facilitating a more effective binding affinity. Additionally, the compound's carboxylic acid moiety plays a crucial role in ionic interactions, influencing the overall kinetics of the enzymatic reaction and modulating inflammatory pathways. | ||||||
Tryptanthrin | 13220-57-0 | sc-202844 sc-202844A | 1 mg 5 mg | $50.00 $213.00 | ||
Tryptanthrin demonstrates selective COX-2 inhibition by engaging in specific hydrogen bonding with key amino acid residues within the enzyme's active site. Its indole structure allows for unique π-π interactions, enhancing binding stability. The compound's electron-rich regions facilitate charge transfer interactions, which can modulate the enzyme's conformational dynamics. This results in altered reaction kinetics, impacting the overall enzymatic activity and influencing inflammatory signaling pathways. | ||||||
Tolfenamic Acid | 13710-19-5 | sc-204918 sc-204918A | 5 g 25 g | $69.00 $312.00 | ||
Tolfenamic Acid exhibits selective inhibition of COX-2 through its unique structural features, including a carboxylic acid group that forms strong ionic interactions with the enzyme's active site. The presence of an aromatic ring enhances π-stacking interactions, contributing to binding affinity. Additionally, its hydrophobic regions promote van der Waals interactions, influencing the enzyme's conformational flexibility and altering substrate accessibility, thereby affecting enzymatic turnover rates. | ||||||
Ibuprofen | 15687-27-1 | sc-200534 sc-200534A | 1 g 5 g | $52.00 $86.00 | 6 | |
Ibuprofen selectively targets COX-2 by engaging in specific hydrogen bonding with key amino acid residues in the enzyme's active site. Its unique hydrophobic alkyl chain facilitates enhanced lipophilicity, allowing for deeper penetration into the enzyme's binding pocket. The compound's conformational adaptability enables it to stabilize transient enzyme states, modulating reaction kinetics and influencing the overall catalytic efficiency of the COX-2 pathway. | ||||||
Ketoprofen | 22071-15-4 | sc-205359 sc-205359A | 5 g 25 g | $93.00 $308.00 | 2 | |
Ketoprofen exhibits selective inhibition of COX-2 through its unique structural features, including a carboxylic acid group that forms ionic interactions with the enzyme's active site. Its aromatic ring enhances π-π stacking interactions, promoting a stable binding conformation. The compound's steric hindrance influences the enzyme's conformational dynamics, effectively altering substrate accessibility and modulating the catalytic turnover rate within the COX-2 pathway. | ||||||
(S)-Ketoprofen | 22161-81-5 | sc-200624 | 1 g | $116.00 | ||
(S)-Ketoprofen demonstrates a distinctive mechanism of action as a COX-2 inhibitor, characterized by its ability to engage in hydrogen bonding with key amino acid residues in the enzyme's active site. The presence of a chiral center contributes to its stereoselectivity, influencing binding affinity. Additionally, the compound's hydrophobic regions facilitate van der Waals interactions, enhancing its stability within the enzyme's pocket and impacting the overall reaction kinetics in the inflammatory pathway. | ||||||
Naproxen | 22204-53-1 | sc-200506 sc-200506A | 1 g 5 g | $24.00 $40.00 | ||
Naproxen exhibits a unique profile as a COX-2 inhibitor, primarily through its ability to form strong π-π stacking interactions with aromatic residues in the enzyme's active site. Its structural rigidity, stemming from its fused ring system, allows for optimal spatial orientation, enhancing binding efficiency. Furthermore, the compound's hydrophilic and lipophilic balance promotes effective solvation dynamics, influencing its interaction kinetics and selectivity within the inflammatory cascade. |