L5170
Leukotriene A4 Hydrolase human
recombinant, expressed in E. coli
Synonym(s):
LTA-4 hydrolase, LTA4, LTA4H
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
recombinant
expressed in E. coli
description
contains C-terminal his-tag
Assay
≥90% (SDS-PAGE)
mol wt
~69 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... LTA4H(4048)
Application
Leukotriene A4 Hydrolase human (LTA4H) is a drug target for anti-inflammation, and for cancer prevention and therapy. It is also suitable for screening inhibitors of Leukotriene B4 synthesis. LTA4H is used to study allergic asthma and airway hyperresponsiveness .
Biochem/physiol Actions
Leukotriene A4 Hydrolase human (LTA4H) is a bifunctional zinc metalloenzyme that converts LTA4 into Leukotriene B4, and also demonstrates aminopeptidase activity. Leukotriene B4 is a lipid chemoattractant that plays critical roles in inflammaton, immune responses, host defenses against infections, and lipid homeostasis. Inhibition of LTA4H in a mouse model decreases LTB4 in the airways and attenuates airway inflammation and airway hyperreactivity through modulation of T cell and dendritic cell function .
Physical form
Supplied as a solution in 100mM Tris, pH 8.0, containing 20% glycerol and 100mM potassium chloride.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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J Haeggström et al.
The Journal of biological chemistry, 261(14), 6332-6337 (1986-05-15)
Mouse liver homogenates transformed leukotriene A4 into a 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid. This novel enzymatic metabolite of leukotriene A4 was characterized by physical means including ultraviolet spectroscopy, high performance liquid chromatography, and gas chromatography-mass spectrometry. After subcellular fractionation, the enzymatic activity was
John W Newman et al.
Progress in lipid research, 44(1), 1-51 (2005-03-08)
The epoxide hydrolases (EHs) are enzymes present in all living organisms, which transform epoxide containing lipids by the addition of water. In plants and animals, many of these lipid substrates have potent biologically activities, such as host defenses, control of
L Orning et al.
The Journal of biological chemistry, 269(15), 11269-11273 (1994-04-15)
Leukotriene-A4 hydrolase (EC 3.3.2.6) cleaved the NH2-terminal amino acid from several tripeptides, typified by arginyl-glycyl-aspartic acid, arginyl-glycyl-glycine, and arginyl-histidyl-phenylalanine, with catalytic efficiencies (kcat/Km) > or = 1 x 10(6) M-1 s-1. This exceeds by 10-fold the kcat/Km for its lipid
A J Fretland et al.
Chemico-biological interactions, 129(1-2), 41-59 (2001-01-13)
Epoxides are organic three-membered oxygen compounds that arise from oxidative metabolism of endogenous, as well as xenobiotic compounds via chemical and enzymatic oxidation processes, including the cytochrome P450 monooxygenase system. The resultant epoxides are typically unstable in aqueous environments and
N Ohishi et al.
The Journal of biological chemistry, 262(21), 10200-10205 (1987-07-25)
Leukotriene A4 hydrolase from the human lung was purified to apparent homogeneity. The molecular weight (68,000-71,000), the amino acid composition, and the N-terminal amino acid sequence were similar to those of the human neutrophil enzyme but different from those of
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