Date published: 2025-10-3

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5-LO Inhibitors

Santa Cruz Biotechnology now offers a broad range of 5-LO Inhibitors. 5-lipoxygenase (5-LO) is expressed primarily in polymorphonuclear leukocytes, macrophages, and mast cells. 5-LO performs the first two catalytic reactions in the biosynthesis of leukotrienes. 5-LO Inhibitors offered by Santa Cruz inhibit 5-LO and, in some cases, other leukotriene and lipid metabolite biosynthesis related proteins. View detailed 5-LO Inhibitor specifications, including 5-LO Inhibitor CAS number, molecular weight, molecular formula and chemical structure, by clicking on the product name.

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Items 51 to 53 of 53 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

YS121

916482-17-2sc-296707
sc-296707A
1 mg
5 mg
$56.00
$251.00
(0)

YS121 serves as a selective inhibitor of 5-lipoxygenase, characterized by its unique molecular architecture that enhances binding affinity to the enzyme's active site. This compound exhibits distinct kinetic behavior, influencing the rate of leukotriene synthesis through competitive inhibition. Its specific interactions with key amino acid residues within the enzyme facilitate altered conformational dynamics, potentially impacting downstream signaling pathways and metabolic regulation.

ZLJ-6

1051931-39-5sc-224468
sc-224468A
1 mg
5 mg
$40.00
$180.00
(0)

ZLJ-6 functions as a potent 5-lipoxygenase inhibitor, distinguished by its unique structural features that promote strong interactions with the enzyme's active site. This compound demonstrates remarkable reaction kinetics, exhibiting a non-competitive inhibition profile that alters the enzyme's catalytic efficiency. Its selective binding induces conformational changes, affecting substrate accessibility and modulating the overall leukotriene biosynthetic pathway, thereby influencing cellular signaling mechanisms.

CAY10589

1077626-52-8sc-223872
sc-223872A
1 mg
5 mg
$56.00
$255.00
(0)

CAY10589 acts as a selective 5-lipoxygenase inhibitor, characterized by its ability to form stable interactions with key residues in the enzyme's active site. This compound exhibits unique reaction kinetics, demonstrating a time-dependent inhibition that enhances its efficacy over prolonged exposure. Its distinct molecular architecture facilitates specific hydrogen bonding and hydrophobic interactions, ultimately disrupting the enzyme's normal function and influencing lipid mediator production.