|Related Categories||Alphabetical Index, Antibodies, Antibodies for Alzheimer′s Disease, Antibodies for Cell Biology, Antibodies for Hematopoietic Stem Cells,|
|species reactivity||yeast, Xenopus, human, rat, bovine, Caenorhabditis elegans, Drosophila, mouse, hamster|
|immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable|
|indirect ELISA: suitable|
|western blot: 1:10,000 using rat brain extract|
|antibody form||ascites fluid|
|mol wt||antigen ERK-1 mol wt 44 kDa|
|antigen ERK-2 mol wt 42 kDa|
|contains||15 mM sodium azide|
|shipped in||dry ice|
human ... MAPK1(5594), MAPK3(5595)|
mouse ... Mapk1(26413), Mapk3(26417)
rat ... Mapk1(116590), Mapk3(50689)
synthetic peptide HTGFLpTEpYVAT corresponding to the phosphorylated form of the ERK-activation loop.
MAP kinase (MAPK, mitogen-activated protein kinase, also termed ERK, extracellular regulated protein kinase), consists of a family of protein kinases which are considered to play a crucial role in various signal transduction pathways leading signals of growth factor, as well as G protein-coupled receptors to their intracellular targets. MAP kinase was shown to regulate several cellular processes among them proliferation, differentiation, cellular morphology and oncogenesis.
Molecular cloning has established that MAP kinase (ERKs) consists of at least four isoforms: ERK-1 (p44mapk), ERK-2 (p42mapk), ERK-3, and ERK-5.
Activation of ERK-1 and ERK-2 in mitogen-stimulated cells is directly mediated by MAP kinase kinase (MAPKK or MEK), a dual-specificity protein kinase, which phosphorylates both threonine and tyrosine residues in the regulatory sites of MAP kinase. Following activation, MAP kinase phosphorylates several nuclear targets, including transcription factors as well as membrane and cytoskeletal proteins. Termination of MAP kinase signalling appears to be mediated by MAP kinase phosphatase, MKP-1, a dual specificity Thr/Tyr phosphatase which dephosphorylates and inactivates MAP kinase. MAP kinase isoforms appear to be widely expressed, in the central nervous system, thymus, spleen, heart, lung, kidney, and are expressed in high levels in PC12 cells and in fibroblasts.
The antibody reacts specifically with the diphosphorylated form of MAP kinase (ERK-1 and ERK-2). It does not recognize the non-phosphorylated or the monophosphorylated forms of MAP kinase or the diphosphorylated forms of JNK and p38 MAP kinase. The epitope recognized by the antibody contains the phosphorylated threonine and tyrosine residues within the regulatory site of active MAP kinase.
Antibodies that react specifically with the active form of MAP kinase are useful for the study of the specific activation requirements, differential tissue expression, and intracellular localization of the active form of MAP kinase in normal and neoplastic tissue.
Monoclonal Anti-MAP Kinase, Activated (Diphosphorylated ERK-1&2) may be used for the localization of the active, dually-phosphorylated, form of MAP kinase using various immunochemical assays such as immunoblotting of cultured cells and tissue extracts, ELISA, immunocytochemistry, immunoprecipitation, and in immunohistochemistry (formalin and formaldehyde-fixed sections). Reactivity has been observed with human, bovine, rat, mouse, Drosophila, Spodoptera frugiperda, and yeast.
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affinity isolated antibody, buffered aqueous solution
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Alzheimer's disease (AD) is the most common cause of dementia in the elderly and is characterized by gradual loss of cognitive functions. Hallmark pathohistological findings of AD include widespread ...
Carolyn L. Crankshaw
BioFiles v7 n2, 2011, 4–8
Keywords: Alzheimer Disease, Gene expression, Genetic, Genetics, Inflammation, Metabolism, Phosphorylations
As a leading supplier of antibodies, Sigma® Life Science is committed to providing researchers the antibody they need with the quality they deserve. Our Antibody Explorer Search Tool provides easy ac...
Keywords: Buffers, Cell biology, Epigenetics, Immunohistochemistry, Immunoprecipitation, Molecular biology, Neuroscience, Western blot
Signal Strength Dictates Phosphoinositide 3-Kinase Contribution to Ras/Extracellular Signal-Regulated Kinase 1 and 2 Activation via Differential Gab1/Shp2 Recruitment: Consequences for Resistance to Epidermal Growth Factor Receptor Inhibition Montagner, A., et al. Mol. Cell. Biol. 28, 587-600, (2008)
Damage-induced Activation Of ERK1/2 In Cochlear Supporting Cells Is A Hair Cell Death-promoting Signal That Depends On Extracellular ATP And Calcium. Lahne, M., and Gale, J.E. J. Neurosci. 28, 4918-28, (2008)
Bevacizumab/docetaxel association is more efficient than docetaxel alone in reducing breast and prostate cancer cell growth: a new paradigm for understanding the therapeutic effect of combined treatment. Ortholan, C., et al. Eur. J. Cancer 46, 3022-36, (2010)
Lipopolysaccharide initiates inflammation in bovine granulosa cells via the TLR4 pathway and perturbs oocyte meiotic progression in vitro. Bromfield, J.J., and Sheldon, I.M. Endocrinology 152, 5029-40, (2011)
PPAR-gamma agonist ameliorates kidney and liver disease in an orthologous rat model of human autosomal recessive polycystic kidney disease. Yoshihara, D., et al. Am. J. Physiol. Renal Physiol. 300, F465-74, (2011)
Protein Arginine Methyltransferase 5 (PRMT5) Signaling Suppresses Protein Kinase Cδ- and p38δ-dependent Signaling and Keratinocyte Differentiation. Kanade, S.R., and Eckert, R.L. J. Biol. Chem. 287, 7313-23, (2012)
Neuroprotection by NMDA preconditioning against glutamate cytotoxicity is mediated through activation of ERK 1/2, inactivation of JNK, and by prevention of glutamate-induced CREB inactivation. Navon, H., et al. J. Mol. Neurosci. 46, 100-8, (2012)
Toll-like receptor 4 and MYD88-dependent signaling mechanisms of the innate immune system are essential for the response to lipopolysaccharide by epithelial and stromal cells of the bovine endometrium. Cronin, J.G., et al. Biol. Reprod. 86, 51, (2012)
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