Human LTA4H, His Tag (LTH-H5220) is expressed from human 293 cells (HEK293). It contains AA Met 1 - Asp 611 (Accession # NP_000886.1).
Predicted N-terminus: Met 1
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 70.1 kDa. The protein migrates as 62-72 kDa under reducing (R) condition (SDS-PAGE).
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 20 mM HEPES, 100 mM NaCl, pH7.3. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
No activity loss is observed after storage at:
- 4-8°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human LTA4H, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Leukotriene A4 hydrolase (LTA4H) is a protein which belongs to the peptidase M1 family, specifically those acting on ether bonds (ether hydrolases). LTA4H is bifunctional enzyme which converts leukotriene A4 to leukotriene B4 and acts as an aminopeptidase. LTA4H participates in arachidonic acid metabolism. LTA4H is inhibited by bestatin and subject to suicide inhibition by leukotriene A4, due to the formation of a covalent adduct at Tyr-379. LTA4H binds 1 zinc ion per subunit.
- (1) Odlander B., et al., 1991, Arch. Biochem. Biophys. 287:167-174.
- (2) Mueller M.J., et al., 1995, Proc. Natl. Acad. Sci. U.S.A. 92:8383-8387.
- (3) Thunnissen M.M., et al., 2002, FASEB J. 16:1648-1650.
- (4) Rudberg P.C., et al., 2002, Proc. Natl. Acad. Sci. U.S.A. 99:4215-4220.
- (5) Rudberg P.C., et al., 2004, J. Biol. Chem. 279:27376-27382.
- (6) Tholander F., et al., 2008, Chem. Biol. 15:920-929.
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