Összes fotó(2)
Fontos dokumentumok
M3807
Anti-MAP Kinase, Non-Phosphorylated ERK antibody, Mouse monoclonal
clone ERK-NP2, purified from hybridoma cell culture
Szinonimák:
Anti-ERK, Anti-ERK-2, Anti-ERK2, Anti-ERT1, Anti-MAPK2, Anti-NS13, Anti-P42MAPK, Anti-PRKM1, Anti-PRKM2, Anti-p38, Anti-p40, Anti-p41, Anti-p41mapk, Anti-p42-MAPK
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(2)
About This Item
konjugátum:
unconjugated
application:
ARR
ELISA (i)
ICC
WB
ELISA (i)
ICC
WB
klón:
ERK-NP2, monoclonal
faj reaktivitás:
human, rat
citations:
19
technika/technikák:
immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 5-25 μg/mL using rat brain extract
indirect ELISA: suitable
microarray: suitable
western blot: 5-25 μg/mL using rat brain extract
Javasolt termékek
biológiai forrás
mouse
Minőségi szint
konjugátum
unconjugated
antitest forma
purified from hybridoma cell culture
antitest terméktípus
primary antibodies
klón
ERK-NP2, monoclonal
Forma
buffered aqueous solution
molekulatömeg
antigen, ERK-1 44 kDa
antigen, ERK-2 42 kDa
faj reaktivitás
human, rat
koncentráció
~2 mg/mL
technika/technikák
immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 5-25 μg/mL using rat brain extract
izotípus
IgG1
UniProt elérési szám
kiszállítva
dry ice
tárolási hőmérséklet
−20°C
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... MAPK1(5594) , MAPK3(5595)
rat ... Mapk1(116590) , Mapk3(50689)
Related Categories
Általános leírás
Mitogen-activated protein kinase (MAPK) superfamily of enzymes is involved in widespread signalling pathways. Members of this family include the ERK1/2 (extracellular signal-regulated protein kinase, also termed p42/p44 MAPK), JNK and p38 MAPK subfamilies. These are the terminal enzymes in a signalling cascade where each kinase phosphorylates and activates the next member in the sequence. Phosphorylation of both tyrosine and threonine is essential for the full activation of all MAPKs. Several kinases participate in activation of the ERK cascade. This cascade is initiated by the small G protein Ras, which upon stimulation causes activation Raf1 kinase. Raf1 continues the transmission by activating MEK. Activated MEK appears to be the only kinase capable of specifically phosphorylating and activating ERK. ERK appears to be an important regulatory molecule, which by can phosphorylate regulatory targets in the cytosol (phospholipase A2, PLA2), translocated into and phosphorylate substrates in the nucleus (ELK1). The activation of ERK cascade mediates and regulates the signal transduction pathways in response to stress, mitogenic signals and is important in development and differentiation, learning, memory and survival.
Egyediség
The antibody reacts specifically with the non-phosphorylated, non-activated form of MAP kinase (ERK-1 and ERK-2). Weak cross-reaction is observed with monophosphorylated (threonine or tyrosine), but not with diphosphorylated peptides of MAPK. The antibody does not recognize JNK or p38 MAPK. The epitope recognized by the antibody contains non-phosphorylated threonine 183 and tyrosine 185 which resides within the ERK-activation loop (e.g., amino acids 178-188 in ERK-2).
Immunogén
synthetic peptide HTGFLTEYVAT, corresponding to the non-phosphorylated form of ERK-activation loop.
Alkalmazás
A working concentration of 5-25 μg/mL may be used for detection by immunoblotting in rat brain extract. The antibody has also been used at working dilution of 1:50 for MAPK quantification by flow cytometry in monocyte-derived macrophages (MDM) derived from Holstein cattle.
Fizikai forma
Solution in phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Elkészítési megjegyzés
Prepared from a culture supernatant of bioreactor grown hybridoma
Jogi nyilatkozat
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Tárolási osztály kódja
10 - Combustible liquids
WGK
nwg
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
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Margarita Arango-Lievano et al.
Molecular and cellular biology, 36(6), 1019-1031 (2016-01-21)
Palmitoylation is involved in several neuropsychiatric and movement disorders for which a dysfunctional signaling of the dopamine D3 receptor (Drd3) is hypothesized. Computational modeling of Drd3's homologue, Drd2, has shed some light on the putative role of palmitoylation as a
Raffaella Molteni et al.
Neural plasticity, 2016, 2592319-2592319 (2016-02-18)
Although activity-dependent transcription represents a crucial mechanism for long-lasting experience-dependent changes in the hippocampus, limited data exist on its contribution to pathological conditions. We aim to investigate the influence of chronic stress on the activity-dependent transcription of brain-derived neurotrophic factor
Xin Wan et al.
Molecular medicine reports, 9(1), 229-234 (2013-10-23)
In this study, the role of the endothelin B receptor (ETBR) in oligodendroglioma cell proliferation and survival was investigated in vitro and in vivo. The overexpression and knockdown of ETBR was conducted in Hs683 human oligodendroglioma cells, and cell proliferation and activation (phosphorylation)
Michelle C Mendoza et al.
Trends in biochemical sciences, 36(6), 320-328 (2011-05-03)
The Ras-extracellular signal-regulated kinase (Ras-ERK) and phosphatidylinositol 3-kinase-mammalian target of rapamycin (PI3K-mTOR) signaling pathways are the chief mechanisms for controlling cell survival, differentiation, proliferation, metabolism, and motility in response to extracellular cues. Components of these pathways were among the first
Z Yao et al.
FEBS letters, 468(1), 37-42 (2000-02-23)
When cells are stimulated by mitogens, extracellular signal-regulated kinase (ERK) is activated by phosphorylation of its regulatory threonine (Thr) and tyrosine (Tyr) residues. The inactivation of ERK may occur by phosphatase-mediated removal of the phosphates from these Tyr, Thr or
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