Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|M, R||IP, WB||Rb||Purified||Monoclonal Antibody|
|Description||Anti-MAP Kinase 1/Erk 1 Antibody, CT, rabbit monoclonal|
|Application||Detect MAP Kinase 1/Erk 1 using this Anti-MAP Kinase 1/Erk 1 Antibody, CT validated for use in IP & WB.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||2 years at -20°C from date of shipment|
|Material Size||100 µL|
|Anti-MAP Kinase 1/Erk 1, CT - 30627||30627|
|Reference overview||Pub Med ID|
|Fibroblast growth factor 22 is not essential for skin development and repair but plays a role in tumorigenesis.|
Jarosz, M; Robbez-Masson, L; Chioni, AM; Cross, B; Rosewell, I; Grose, R
PloS one 7 e39436 2012
Fibroblast Growth Factors play critical roles during development, tissue homeostasis and repair by controlling cell proliferation, survival, migration and differentiation. Of the 22 mammalian FGFs, FGF22, a member of the FGF7/10/22 subfamily, has been shown to have a clear role in synaptogenesis, but its roles in other tissues have not been studied. We have investigated the in vivo functions of FGF22 in mice. Fgf22 null animals were viable, fertile and did not display any obvious abnormalities. Despite the known expression profile of FGF22 in the skin, no differences in either skin or pelage were observed, demonstrating that FGF22 is dispensable during embryogenesis and in unchallenged adult skin. Mice lacking FGF22 were able to heal acute wounds just as efficiently as wild type mice. However, classical two-step skin carcinogenesis challenge revealed that FGF22 null mice developed fewer papillomas than wild type controls, suggesting a potential pro-oncogenic role for FGF22 in the skin.
|Isoelectric focusing technology quantifies protein signaling in 25 cells.|
O'Neill, RA; Bhamidipati, A; Bi, X; Deb-Basu, D; Cahill, L; Ferrante, J; Gentalen, E; Glazer, M; Gossett, J; Hacker, K; Kirby, C; Knittle, J; Loder, R; Mastroieni, C; Maclaren, M; Mills, T; Nguyen, U; Parker, N; Rice, A; Roach, D; Suich, D; Voehringer, D; Voss, K; Yang, J; Yang, T; Vander Horn, PB
Proceedings of the National Academy of Sciences of the United States of America 103 16153-8 2006
A previously undescribed isoelectric focusing technology allows cell signaling to be quantitatively assessed in less than 25 cells. High-resolution capillary isoelectric focusing allows isoforms and individual phosphorylation forms to be resolved, often to baseline, in a 400-nl capillary. Key to the method is photochemical capture of the resolved protein forms. Once immobilized, the proteins can be probed with specific antibodies flowed through the capillary. Antibodies bound to their targets are detected by chemiluminescence. Because chemiluminescent substrates are flowed through the capillary during detection, localized substrate depletion is overcome, giving excellent linearity of response across several orders of magnitude. By analyzing pan-specific antibody signals from individual resolved forms of a protein, each of these can be quantified, without the problems associated with using multiple antibodies with different binding avidities to detect individual protein forms.
|The Ras-MAPK signal transduction pathway, cancer and chromatin remodeling.|
Dunn, Katherine L, et al.
Biochem. Cell Biol., 83: 1-14 (2005) 2005
Stimulation of the Ras-mitogen-activated protein kinase (MAPK) signal transduction pathway results in a multitude of events including expression of the immediate-early genes, c-fos and c-myc. Downstream targets of this stimulated pathway are the mitogen- and stress-activated protein kinases (MSK) 1 and 2, which are histone H3 kinases. In chromatin immunoprecipitation assays, it has been shown that the mitogen-induced phosphorylated H3 is associated with the immediate-early genes and that MSK1/2 activity and H3 phosphorylation have roles in chromatin remodeling and transcription of these genes. In oncogene-transformed fibroblasts in which the Ras-MAPK pathway is constitutively active, histone H1 and H3 phosphorylation is increased and the chromatin of these cells has a more relaxed structure than the parental cells. In this review we explore the deregulation of the Ras-MAPK pathway in cancer, with an emphasis on breast cancer. We discuss the features of MSK1 and 2 and the impact of a constitutively activated Ras-MAPK pathway on chromatin remodeling and gene expression.
|Wiring diagrams of MAPK regulation by MEKK1, 2, and 3.|
Uhlik, Mark T, et al.
Biochem. Cell Biol., 82: 658-63 (2004) 2004
Mitogen-activated protein kinase (MAPK) pathways are activated by a plethora of stimuli. The literature is filled with papers describing the activation of different MAPKs by almost any stimulus or insult imaginable to cells. In this review, we use signal transduction wiring diagrams to illustrate putative upstream regulators for the MAPK kinase kinases, MEKK1, 2, and 3. Targeted gene disruption of MEKK1, 2, or 3 defined phenotypes for each MEKK associated with loss of specific MAPK regulation. Genetic analysis of MEKK function clearly defines specific components of the wiring diagram that require MEKK1, 2, or 3 for physiological responses. We propose that signal transduction network wiring diagrams are valuable tools for hypothesis building and filtering physiologically relevant phenotypic responses from less connected protein relations in the regulation of MAPK pathways.
|ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions.|
Roux, Philippe P and Blenis, John
Microbiol. Mol. Biol. Rev., 68: 320-44 (2004) 2004
Conserved signaling pathways that activate the mitogen-activated protein kinases (MAPKs) are involved in relaying extracellular stimulations to intracellular responses. The MAPKs coordinately regulate cell proliferation, differentiation, motility, and survival, which are functions also known to be mediated by members of a growing family of MAPK-activated protein kinases (MKs; formerly known as MAPKAP kinases). The MKs are related serine/threonine kinases that respond to mitogenic and stress stimuli through proline-directed phosphorylation and activation of the kinase domain by extracellular signal-regulated kinases 1 and 2 and p38 MAPKs. There are currently 11 vertebrate MKs in five subfamilies based on primary sequence homology: the ribosomal S6 kinases, the mitogen- and stress-activated kinases, the MAPK-interacting kinases, MAPK-activated protein kinases 2 and 3, and MK5. In the last 5 years, several MK substrates have been identified, which has helped tremendously to identify the biological role of the members of this family. Together with data from the study of MK-knockout mice, the identities of the MK substrates indicate that they play important roles in diverse biological processes, including mRNA translation, cell proliferation and survival, and the nuclear genomic response to mitogens and cellular stresses. In this article, we review the existing data on the MKs and discuss their physiological functions based on recent discoveries.
|Regulatory mechanisms and function of ERK MAP kinases.|
Torii, Satoru, et al.
J. Biochem., 136: 557-61 (2004) 2004
Spatiotemporal control of the Ras/ERK MAP kinase signaling pathway is a key factor for determining the specificity of cellular responses including cell proliferation, cell differentiation and cell survival. The fidelity of this signaling is regulated by docking interactions as well as scaffolding. Subcellular localization of ERK is controlled by cytoplasmic ERK anchoring proteins that have a nuclear export signal (NES), such as MEK. In quiescent cells, ERK and MEK localize to the cytoplasm. In response to stimulation, dissociation of the MEK-ERK complex is induced and activated ERK translocates to the nucleus. Recently, several negative regulators for Ras/ERK signaling have been identified and their detailed molecular mechanisms have been analyzed. Among them, Sprouty and Sef act as a temporal and a spatial regulator, respectively, for Ras/ERK signaling. Thus, multiple factors are involved in control of Ras/ERK signaling.