Product Pathways - Neuroscience
MELK Antibody #2274
| Applications | Reactivity | MW (kDa) | Source |
|---|---|---|---|
| W IP | H M Dr | 74 | Rabbit |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
Reactivity Key:
H=Human
M=Mouse
Dr=Drosophila
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
MELK antibody detects endogenous levels of total MELK protein.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to amino acids near the carboxy-terminus of human MELK. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts of jurkat and K562 cells, using MELK Antibody.
Background
MELK (Maternal Embryonic Leucine zipper Kinase, MPK38, KIAA0175) is a member of the Snf1/AMPK related kinase family. It is implicated in stem cell renewal, cell cycle progression and pre-m-RNA splicing (1,2,3). MELK is also a marker for self-renewing multipotent neural progenators, and may function in embryonic and postnatal forebrain development (4). While other members of this kinase family are activated by LKB1 and CAMKII mediated phosphorylation of the T-loop, MELK is not (5,6,7). Regulation of activation appears complex since MELK overexpressed in mammalian cells is inactive (7). Some evidence suggests that activation occurs through autophosphorylation of Thr167 and Ser171, although a number of additional autophosphorylation sites have been suggested (8). Recently, phosphorylations of Thr449, Thr451 and Thr481 have been specifically detected during mitosis, and are thought to occur via MPF and MAPK pathways (9). MELK has broad substrate specificity in vitro: substrates include ZPR9 (10), NIPP1 (11) and cdc25B (12), although the significance of MELK mediated phosphorylation of these proteins is unclear.Finally, recent studies on human tumor samples and cell lines suggest that MELK expression is frequently elevated in cancer relative to normal tissues (13). MELK may provide a growth advantage for neoplastic cells, and may be a potential target for anti-cancer therapies.
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- Davezac, N. et al. (2002) Oncogene 21, 7630-41.
- Vulsteke, V. et al. (2004) J. Biol. Chem. 279, 8642-7.
- Nakano, I. et al. (2005) J. Cell Biol. 170, 413-27.
- Tassan, J.P. and Le Goff, X. (2004) Biol. Cell 96, 193-9.
- Woods, A. et al. (2003) Curr. Biol. 13, 2004-8.
- Lizcano, J.M. et al. (2004) EMBO J. 23, 833-43.
- Beullens, M. et al. (2005) J. Biol. Chem. 280, 40003-11.
- Badouel, C. et al. (2006) Cell Cycle. 5, 883-889.
- Seong, H.A. et al. (2002) Biochem. J. 361, 597-604.
- Vulsteke, V. et al. (2004) J. Biol. Chem. 279, 8642-7.
- Davezac, N. et al. (2002) Oncogene 21, 7630-41.
- Gray, D. et al. (2005) Cancer Res. 65, 9751-61.
Application References
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