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MetAP2 (human), (recombinant) (HA-tag)

BML-SE569-0010 10 µg 472.00 USD
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Product Details

Alternative Name:Methionine aminopeptidase 2, p67eIF2, Eukaryotic initiation factor 2-associated protein
Source:Produced in insect cells. Recombinant, full-length (aa 1-478) methionine aminopeptidase 2 with an N-terminal hemagglutinin (HA) tag (YPYDVPDYA), cloned from human cDNA. Produced in a baculovirus expression system.
UniProt ID:P50579
Formulation:Liquid. In 20mM HEPES, pH 7.3, containing 0.1M KCl, 1mM CoCl2, 1.5mM MgCl2, 0.02% sodium azide and 10% glycerol.
Purity:≥95% (SDS-PAGE)
Purity Detail:Purified by chromatography
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:Stable for at least 6 months after receipt when stored at -80°C.
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
Scientific Background:MetAP2 is a metalloenzyme that catalyzes removal of the N-terminal methionine from proteins, with the physiologically relevant metal thought to be either cobalt or manganese. Since it was identified as the target of the anti-angiogenic natural product fumagilin (Prod. No. BML-CT100), it has been studied for its involvement in cancer, angiogenesis, inflammation, and rheumatoid arthritis. Because of differing substrate specificities and kinetics it is not desirable to substitute bacterial methionine aminopeptidase for mammalian MetAP2.
Regulatory Status:RUO - Research Use Only
Manufacturer:Mediomics under patents 5,885,820 and 5,888,796

General Literature References

An inhibitor of methionine aminopeptidase type-2, PPI-2458, ameliorates the pathophysiological disease processes of rheumatoid arthritis: D.D. Lazarus, et al.; Inflamm. Res. 57, 18 (2008), Abstract;
An orally delivered small-molecule formulation with antiangiogenic and anticancer activity: O. Benny, et al.; Nat. Biotechnol. 26, 799 (2008), Abstract;
Highly potent inhibitors of methionine aminopeptidase-2 based on 1,2,4-triazole pharmacophore: J.P. Marino, Jr., et al.; J. Med. Chem. 50, 3777 (2007), Abstract;
A methionine aminopeptidase-2 inhibitor, PPI-2458, for the treatment of rheumatoid arthritis: S.G. Bernier, et al.; PNAS USA 101, 10768 (2004), Abstract;
Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese: J. Wang, et al.; Biochemistry 42, 5035 (2003), Abstract;
Proteomics-based target identification: bengamides as a new class of methionine aminopeptidase inhibitors: H. Towbin, et al.; J. Biol. Chem. 278, 52964 (2003), Abstract; Full Text
Structure of human methionine aminopeptidase-2 complexed with fumagillin: S. Liu, et al.; Science 282, 1324 (1998), Abstract;
The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase: W.T. Lowther, et al.; PNAS USA 95, 12153 (1998), Abstract; Full Text
Evidence that the human homologue of rat initiation factor associated protein (p67) is a methionine aminopeptidase: X. Li & Y.-H. Chang; BBRC 227, 152 (1996), Abstract;
Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes: S.M. Arfin, et al.; PNAS USA 92, 7714 (1995), Abstract;

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