NME1/NDKA (G19) Antibody

3338:

Western Blotting

NM23-H1/H2 (G19) Antibody detects endogenous levels of total NM23-H1/H2 protein.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to Gly19 of human NM23-H1/H2. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from various cell lines using NM23-H1/H2 (G19) Antibody.

The NDK/NME/NM23 kinase family (encoded by the NME gene family) consists of at least eight distinct proteins that exhibit different cellular localization (1). Members of this group inhibit metastasis in a variety of tumor cell types (2). All NDK/NME/NM23 proteins possess nucleoside diphosphatase kinase (NDK) activity and catalyze the phosphorylation of nucleoside diphosphate to the corresponding nucleoside triphosphate to regulate a diverse array of cellular events (3). At least four classes of NDK biochemical activities have been described, including protein-protein interactions (4-6), regulation of GTP-binding protein function (7-9), DNA-associated activities (10,11), and histidine-dependent protein phosphotransferase activity (12). NDK/NME proteins participate in the regulation of a broad spectrum of cellular responses, including development, differentiation, proliferation, endocytosis, and apoptosis (13). Because of its role in metastasis suppression and oncogenesis, NDKA (NME1/NM23-H1) has been widely studied (14). NDKA (NM23-H1) and NDKB (NM23-H2) are encoded by adjacent NME1 and NME2 genes and share 90% sequence identity. Two serine residues (Ser122 and Ser144) on NDKA/NM23-H1 can be phosphorylated by AMPKα1, but only phosphorylation at Ser122 determines whether NDKA channels ATP to AMPKα1. This regulates AMPKα1 activity towards ACC1, an important regulator of fatty acid metabolism (15). Mutation of NDKB/NM23-H2 at Ser122 (S122P) in melanoma cells results in altered phosphoryl transfer activity (16).

1. Lacombe, M.L. et al. (2000) J Bioenerg Biomembr 32, 247-58.
2. Tee, Y.T. et al. (2006) Taiwan J Obstet Gynecol 45, 107-13.
3. Ishikawa, N. et al. (2003) J Bioenerg Biomembr 35, 7-18.
4. Paravicini, G. et al. (1996) Biochem Biophys Res Commun 227, 82-7.
5. Reymond, A. et al. (1999) Oncogene 18, 7244-52.
6. Subramanian, C. et al. (2001) Nat Med 7, 350-5.
7. Zhu, J. et al. (1999) Proc Natl Acad Sci USA 96, 14911-8.
8. Otsuki, Y. et al. (2001) Proc Natl Acad Sci USA 98, 4385-90.
9. Palacios, F. et al. (2002) Nat Cell Biol 4, 929-36.
10. Fan, Z. et al. (2003) Cell 112, 659-72.
11. Postel, E.H. (2003) J Bioenerg Biomembr 35, 31-40.
12. Wagner, P.D. and Vu, N.D. (2000) Biochem J 346 Pt 3, 623-30.
13. Kimura, N. et al. (2000) J Bioenerg Biomembr 32, 309-15.
14. Steeg, P.S. (2004) J Natl Cancer Inst 96, E4.
15. Crawford, R.M. et al. (2006) Mol Cell Biol 26, 5921-31.
16. Schaertl, S. et al. (1999) J Biol Chem 274, 20159-64.

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• 7720 Prestained Protein Marker, Broad Range (Premixed Format)
• 7727 Biotinylated Protein Ladder Detection Pack
• 7003 20X LumiGLO^® Reagent and 20X Peroxide

For Research Use Only. Not For Use In Diagnostic Procedures.