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  • 产品名称：LeukotrieneA4Hydrolase(LTA4H)(AA1-611)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
LeukotrieneA4Hydrolase(LTA4H)(AA1-611)(Active)protein(Histag)
详情介绍：
Characteristics 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).
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured by its ability to cleave the fluorogenic peptide substrate, Arg - 7 - amido - 4 - methylcoumarin (R-AMC). The specific activity is >50 pmol/min/μg, as measured under the described conditions.
Background 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.
Molecular Weight 70.1 kDa
NCBI Accession NP_000886
UniProt P09960
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 20 mM HEPES, 100 mM NaCl, pH 7.3
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Supplier Images
SDS-PAGE (SDS) image for Leukotriene A4 Hydrolase (LTA4H) (AA 1-611) (Active) protein (His tag) (ABIN2181484) Human LTA4H, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained ov...
Background publications Tholander, Muroya, Roques, Fournié-Zaluski, Thunnissen, Haeggström: "Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design." in: Chemistry & biology, Vol. 15, Issue 9, pp. 920-9, 2008 (PubMed).

Rudberg, Tholander, Andberg, Thunnissen, Haeggström: "Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates." in: The Journal of biological chemistry, Vol. 279, Issue 26, pp. 27376-82, 2004 (PubMed).

Thunnissen, Andersson, Samuelsson, Wong, Haeggström: "Crystal structures of leukotriene A4 hydrolase in complex with captopril and two competitive tight-binding inhibitors." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 16, Issue 12, pp. 1648-50, 2002 (PubMed).

Rudberg, Tholander, Thunnissen, Haeggström: "Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms." in: The Journal of biological chemistry, Vol. 277, Issue 2, pp. 1398-404, 2002 (PubMed).

Rudberg, Tholander, Thunnissen, Samuelsson, Haeggstrom: "Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 7, pp. 4215-20, 2002 (PubMed).

Mueller, Wetterholm, Blomster, Jörnvall, Samuelsson, Haeggström: "Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in mechanism-based inactivation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, Issue 18, pp. 8383-7, 1995 (PubMed).

Odlander, Claesson, Bergman, Rådmark, Jörnvall, Haeggström: "Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji: indications of catalytically divergent forms of the enzyme." in: Archives of biochemistry and biophysics, Vol. 287, Issue 1, pp. 167-74, 1991 (PubMed).