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M3557

Sigma-Aldrich

Monoclonal Anti-MAP Kinase, Monophosphorylated Threonine antibody produced in mouse

~2 mg/mL, clone ERK-YNP, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-pT-ERK

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About This Item

MDL number:
UNSPSC Code:
12352203

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

ERK-YNP, monoclonal

form

buffered aqueous solution

mol wt

antigen, ERK-1 44 kDa
antigen, ERK-2 42 kDa

species reactivity

rat, human, mouse

concentration

~2 mg/mL

technique(s)

capture ELISA: suitable
immunocytochemistry: suitable
microarray: suitable
western blot: 5-20 μg/mL using rat brain extract

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

General description

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.
Monoclonal Anti-MAP Kinase, monophosphorylated threonine (pT-ERK) reacts specifically with the monophosphorylated threonine. It weakly reacts with the nonphosphorylated forms of MAP kinase (ERK-1 and ERK-2, 44 kD and 42 kD, respectively). It does not recognize doubly-phosphorylated, and the mono-phosphorylated tyrosine forms of the MAPK molecule, or JNK or p38-MAPK.

Specificity

The antibody reacts with the monophosphorylated threonine MAP kinase (ERK-1 and ERK-2) proteins and weaker with the non-phosphorylated forms of MAP kinases. It does not recognize the diphosphorylated, and the monophosphorylated tyrosine forms of the ERK/MAPK proteins, or the JNK and p38 MAPK. The epitope recognized by the antibody contains the threonine residue within the regulatory site of MAP kinase (e.g.,Thr183 in ERK-2).

Immunogen

synthetic peptide HTGFLTEYVAT, corresponding to the non-phosphorylated form of ERK-activation loop.

Application

Monoclonal Anti-MAP Kinase, monophosphorylated threonine antibody may be used for detection in rat brain extract by immunoblotting at a working concentration of 5-20 μg/mL. In cardiomyocytes, immunoblotting may be performed using a working dilution of 1:10,000 of the antibody. The antibody is also suitable for ELISA, immunocytochemistry and protein microarray.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Preparation Note

Prepared from a culture supernatant of bioreactor grown hybridoma.

Disclaimer

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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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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Peter H Sugden et al.
Cellular signalling, 23(2), 468-477 (2010-11-04)
ERK1 and ERK2 (ERK1/2) are central to the regulation of cell division, growth and survival. They are activated by phosphorylation of the Thr- and the Tyr- residues in their Thr-Glu-Tyr activation loops. The dogma is that dually-phosphorylated ERK1/2 constitute the
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
Gaëlle Pérot et al.
Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc, 27(6), 840-850 (2013-11-30)
The clinical relevance of accurately diagnosing pleomorphic sarcomas has been shown, especially in cases of undifferentiated pleomorphic sarcomas with myogenic differentiation, which appear significantly more aggressive. To establish a new smooth muscle differentiation classification and to test its prognostic value
Michiaki Kohno et al.
Biological & pharmaceutical bulletin, 34(12), 1781-1784 (2011-12-02)
The extracellular signal-regulated kinase (ERK) pathway is a major determinant in the control of diverse cellular processes such as proliferation, survival, and motility. This pathway is often upregulated in human cancers and as such represents an attractive target for mechanism-based
Sudhakaran Prabakaran et al.
Molecular systems biology, 7, 482-482 (2011-04-14)
The functional impact of multisite protein phosphorylation can depend on both the numbers and the positions of phosphorylated sites-the global pattern of phosphorylation or 'phospho-form'-giving biological systems profound capabilities for dynamic information processing. A central problem in quantitative systems biology

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