Anti-MEK1 (Thr386) Antibody
Our Anti-MEK1 (Thr386) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human and rat MEK1 (Thr386) and is antigen affinity purified from pooled serum. It is great for use in WB.
Western blot of human T47D cells showing specific immunolabeling of the ~45 kDa MEK 1 protein phosphorylated at Thr386 in the first lane (-). Phosphospecificity is shown in the second lane (+) where immunolabeling is completely eliminated by blot treatment with lambda phosphatase (λ-Ptase, 1200 units for 30 min).
Click on image to zoom
SKU: p180-386
Ships: 1-2 business days
Product Details
MEK1 (Thr386)
MEK 1 (MAP Kinase Kinase, also known as MKK) is an integral component of the MAP kinase cascade that regulates cell growth and differentiation (Ahn, 1993; Chong et al., 2003). This pathway also plays a key role in synaptic plasticity in the brain (Adams and Sweatt, 2002). Activated MEK 1 acts as a dual specificity kinase phosphorylating both a threonine and a tyrosine residue on MAP kinase (Kyriakis et al., 1991; Seger et al., 1991; Crews et al., 1992). Conversely, there also appears to be a feedback phosphorylation of MEK 1 by MAP kinase. The sites on MEK 1 that are phosphorylated by MAP kinase are Thr-292 and Thr-386 (Mansour et al., 1994).
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
ELISA, WB
Rabbit
MAP2K1
45 kDa
Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr386 of human MEK1, conjugated to keyhole limpet hemocyanin (KLH).
Human
Human, Rat
Bovine, Canine, Chicken, Non-Human Primate, Mouse, Xenopus
AB_2492148
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Prepared from pooled rabbit serum by affinity purification via sequential chromatography on phospho and non-phosphopeptide affinity columns.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
WB: 1:1000
Unconjugated
Specific for endogenous levels of the ~45 kDa MEK 1 protein phosphorylated at Thr386. The immunolabeling is completely eliminated by treatment with λ-phosphatase.
Phosphorylated
Thr386
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
AA589381; Dual specificity mitogen activated protein kinase kinase 1; CFC3; MAP kinase kinase 1; Dual specificity mitogen-activated protein kinase kinase 1; Dual specificity mitogen-activated protein kinase kinase 2; EC 2.7.12.2; ERK activator kinase 1; ERK activator kinase 2; FLJ26075; MAP kinase kinase 2; MAP2K1; MAP2K2; MAPK/ERK kinase 1; MAPK/ERK kinase 2; MAPKK 1; MAPKK1; MAPKK2; MEK 1; MEK1; MEKK1; Mitogen activated protein kinase kinase 1; Mitogen activated protein kinase kinase 2; Mitogen-activated protein kinase kinase 2; p45; MK2; MKK 1; MKK 2; MKK1; MKK2; MP2K1_HUMAN; PRKMK 1; PRKMK 2; Prkmk1; Prkmk2; protein kinase; mitogen-activated; kinase 1 (MAP kinase kinase 1; kinase 1; kinase 2; Protein kinase mitogen activated kinase 1; MAP kinase/Erk kinase 1; Protein kinase mitogen activated kinase 1
Q02750
UniProt Summary: 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. Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation (PubMed:29433126). 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. {ECO:0000269|PubMed:14737111, ECO:0000269|PubMed:17101779, ECO:0000269|PubMed:29433126}.
UniProt Summary: 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. Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation (PubMed:29433126). 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. {ECO:0000269|PubMed:14737111, ECO:0000269|PubMed:17101779, ECO:0000269|PubMed:29433126}.
5604
Blue Ice
- Western Blot Protocol: Download
General References
- Adams JP, Sweatt JD (2002) Molecular psychology: Roles for the ERK MAP kinase cascade in memory. Annual Review of Pharmacology and Toxicology 42:135-163. PMID: 10508514
- Ahn NG (1993) The MAP kinase cascade. Discovery of a new signal transduction pathway. Molecualar and Cellular Biochemistry 127-128:201-209. PMID: 23055506
- Chong H, Vikis HG, Guan KL (2003) Mechanisms of regulating the Raf kinase family. Cellular Signalling 15:463-469. PMID: 9620804
- Crews CM, Alessandrini A, Erikson RL (1992) The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product. Science 258:478-480.PMID: 9620804
- Kyriakis JM, Brautigan DL, Ingebritsen TS, Avruch J (1991) pp54 Microtubule-associated protein-2 kinase requires both tyrosine and serine/threonine phosphorylation for activity. Journal of Biological Chemistry 266:10043-10046.PMID: 9620804
- Seger R, Ahn NG, Boulton TG, Yancopoulos GD, Panayotatos N, Radziejewska E, Ericsson L, Bratlien RL, Cobb MH, Krebs EG (1991) Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophos-phorylation on both tyrosine and threonine residues:Implications for their mechanism of activation. PNAS USA 88:6142-6146.PMID: 9620804

