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Leukotriene A4 Hydrolase / LTA4H Antibody, Rabbit MAb

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    Human LTA4H Antibody Product Information
    Immunogen:Recombinant Human Leukotriene A4 Hydrolase / LTA4H protein (Catalog#10276-H08B)
    Clone ID:455
    Ig Type:Rabbit IgG
    Concentration:
    Endotoxin:
    Formulation:0.2 μm filtered solution in PBS with 5% trehalose
    Preparation:This antibody was obtained from a rabbit immunized with purified, recombinant Human Leukotriene A4 Hydrolase / LTA4H (rh Leukotriene A4 Hydrolase / LTA4H; Catalog#10276-H08B; NP_000886.1; Met 1-Asp 611).
    Other LTA4H Antibody Products
    Leukotriene A4 Hydrolase/LTA4H Background

    Leukotriene A-4 hydrolase, also known as LTA-4 hydrolase, Leukotriene A (4) hydrolase, LTA4H and LTA4, is cytoplasm protein which belongs to the peptidase M1 family. LTA4H hydrolyzes an epoxide moiety of leukotriene A4 (LTA-4) to form leukotriene B4 (LTB-4). This enzyme also has some peptidase activity. The leukotrienes (LTs) are a class of structurally related lipid mediators involved in the development and maintenance of inflammatory and allergic reactions. In the biosynthesis of LTs, arachidonic acid was converted into the unstable intermediate epoxide LTA4, which may in turn be conjugated with glutathione to form the spasmogenic LTC4, or hydrolyzed into the proinflammatory lipid mediator LTB4 in a reaction catalyzed by Leukotriene A4 hydrolase (LTA4H). LTB4 is a classical chemoattractant of human neutrophils and triggers adherence and aggregation of leukocytes to vascular endothelium, and also modulates immune responses. As a bifunctional zinc metalloenzyme, LTA4H also exhibits an anion-dependant arginyl aminopeptidase activity of high efficiency and specificity in addition to its epoxide hydrolase activity. LTA4H is regarded as a therapeutic target for inflammation.

    Human Leukotriene A4 Hydrolase/LTA4H References
  • Mancini, JA. et al.,1995, Eur. J. Biochem. 231: 65-71.
  • Orning, L. et al., 1994, J. Biol. Chem. 269: 11269-73.
  • Rudberg, PC. et al., 2004, J. Biol. Chem. 279: 27376-82.
  • Qiu, H. et al., 2006, Proc. Natl. Acad. Sci. USA. 103: 8161-6.
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