|Application ||WB, E|
|Other Accession||P36506, Q63932, P36507, Q90891, Q05116, Q01986, P29678, P31938, Q63980, Q10664, Q24324|
|Predicted||Mouse, Rat, Rabbit, Hamster, Chicken, Xenopus, C.Elegans, Drosophila|
|Other Names||Dual specificity mitogen-activated protein kinase kinase 1, MAP kinase kinase 1, MAPKK 1, MKK1, ERK activator kinase 1, MAPK/ERK kinase 1, MEK 1, MAP2K1, MEK1, PRKMK1|
|Target/Specificity||This MEK1 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S218/222 of human MEK1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is first purified by protein G affinity chromatography. Then, the antibody fraction is peptide affinity purified in a 2-step procedure with control and phosphorylated peptides. The phospho-specific antibody is eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Bi-Phospho-MEK1(S218/222) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator- activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis.|
|Cellular Location||Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Cytoplasm Nucleus. Membrane; Peripheral membrane protein. Note=Localizes at centrosomes during prometaphase, midzone during anaphase and midbody during telophase/cytokinesis (PubMed:14737111). Membrane localization is probably regulated by its interaction with KSR1 (PubMed:10409742)|
|Tissue Location||Widely expressed, with extremely low levels in brain.|
Provided below are standard protocols that you may find useful for product applications.
MEK1is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is known to play a critical role in mitogen growth factor signal transduction. It phosphorylates and thus activates MAPK1/ERK2 and MAPK2/ERK3. The activation of this kinase itself is dependent on the Ser/Thr phosphorylation by MAP kinase kinase kinases. The inhibition or degradation of this kinase is found to be involved in the pathogenesis of Yersinia and anthrax.
Ohren, J.F., et al., J. Neural Transm. 11(12):1192-1197 (2004). Naegele, S., et al., J. Biol. Chem. 279(44):46023-46034 (2004). Ussar, S., et al., J. Biol. Chem. 279(42):43861-43869 (2004). Beausoleil, S.A., et al., Proc. Natl. Acad. Sci. U.S.A. 101(33):12130-12135 (2004). Spence, H.J., et al., EMBO Rep. 5(5):484-489 (2004).