Datasheet

Biological Description

Specificity	5 Lipoxygenase/5-LO Rabbit mAb detects endogenous levels of total 5 Lipoxygenase/5-LO protein.
Background	5-Lipoxygenase (5-LO) is a non-heme iron-containing monomeric enzyme of the lipoxygenase family that catalyzes the initial steps of leukotriene biosynthesis by oxygenating arachidonic acid into 5-HPETE and subsequently dehydrating it to leukotriene A4 (LTA4). 5-LO is composed of two main domains: an N-terminal β-sandwich C2-like domain responsible for calcium and membrane binding, and a C-terminal catalytic domain housing a non-heme iron coordinated by a 2-His-1-carboxylate facial triad essential for its dioxygenase function. The enzyme is activated by calcium ions, membrane association, and ATP binding, which stabilizes its conformation and enhances enzymatic activity. 5-LO interacts with accessory proteins like coactosin-like protein (CLP) to promote catalysis. The enzyme plays a fundamental role in producing leukotrienes, which are potent lipid mediators regulating inflammation, immune cell chemotaxis, vasoconstriction, and bronchoconstriction. 5-LO expression is primarily in leukocytes, including neutrophils, eosinophils, macrophages, and mast cells. Its activity is tightly regulated transcriptionally and post-translationally through phosphorylation, calcium signaling, and intracellular localization to maintain leukotriene production in response to stimuli. Additionally, 5-LO translocates to the nucleus, where it associates with euchromatin and influences gene expression and microRNA processing independent of its enzymatic role. Dysregulated 5-LO activity is implicated in diseases such as asthma, atherosclerosis, and cancer.

Specificity

5 Lipoxygenase/5-LO Rabbit mAb detects endogenous levels of total 5 Lipoxygenase/5-LO protein.

Background

5-Lipoxygenase (5-LO) is a non-heme iron-containing monomeric enzyme of the lipoxygenase family that catalyzes the initial steps of leukotriene biosynthesis by oxygenating arachidonic acid into 5-HPETE and subsequently dehydrating it to leukotriene A4 (LTA4). 5-LO is composed of two main domains: an N-terminal β-sandwich C2-like domain responsible for calcium and membrane binding, and a C-terminal catalytic domain housing a non-heme iron coordinated by a 2-His-1-carboxylate facial triad essential for its dioxygenase function. The enzyme is activated by calcium ions, membrane association, and ATP binding, which stabilizes its conformation and enhances enzymatic activity. 5-LO interacts with accessory proteins like coactosin-like protein (CLP) to promote catalysis. The enzyme plays a fundamental role in producing leukotrienes, which are potent lipid mediators regulating inflammation, immune cell chemotaxis, vasoconstriction, and bronchoconstriction. 5-LO expression is primarily in leukocytes, including neutrophils, eosinophils, macrophages, and mast cells. Its activity is tightly regulated transcriptionally and post-translationally through phosphorylation, calcium signaling, and intracellular localization to maintain leukotriene production in response to stimuli. Additionally, 5-LO translocates to the nucleus, where it associates with euchromatin and influences gene expression and microRNA processing independent of its enzymatic role. Dysregulated 5-LO activity is implicated in diseases such as asthma, atherosclerosis, and cancer.

Usage Information

Application

WB, IHC, IF, FCM

Dilution

WB	IHC	IF
1:1000 - 1:2000	1:100	1:100

Reactivity

Rat, Human

Source

Rabbit

MW

78 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/10591081/
https://pubmed.ncbi.nlm.nih.gov/18987389/

5 Lipoxygenase/5-LO Rabbit mAb

Biological Description

Usage Information

References

Application Data