Mitogen-Activated Protein Kinase 1/3 (MAPK1/3) (pThr202), (pTyr204) antibody

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Antigen
  • erk1/2
  • mitogen-activated protein kinase
  • erk1/2
Epitope
pThr202, pTyr204
123
121
31
30
30
19
18
15
15
15
15
15
12
9
9
9
9
8
6
5
4
3
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Mouse (Murine), Rat (Rattus), Human
416
316
300
57
23
15
9
8
8
7
7
6
5
5
3
3
2
2
2
1
1
1
1
Host
Rabbit
344
78
7
Clonality
Polyclonal
Conjugate
Un-conjugated
12
11
11
9
7
7
7
7
6
6
6
6
6
6
2
2
2
1
1
1
1
1
1
1
1
Application
Immunohistochemistry (IHC), Western Blotting (WB)
303
112
83
78
60
56
42
42
15
10
6
4
2
2
2
2
2
1
Options
Supplier
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Immunogen A synthetic peptide from the phospho T202 & Y204 of human Erk1, Erk2 conjugated to an immunogenic carrier protein was used as the antigen. The peptide is homologous in many species including rat, mouse, zebra fish, xenopus and chicken.
Isotype IgG
Specificity Specific for Erk1 and Erk2.
Alternative Name Erk1, Erk2 (MAPK1/3 Antibody Abstract)
Background Function: Involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors such as ELK-1. Phosphorylates EIF4EBP1, required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1. Phosphorylates heat shock factor protein 4 (HSF4).
Catalytic activity: ATP + a protein = ADP + a phosphoprotein.
Cofactor: Magnesium.
Enzyme regulation: Activated by tyrosine phosphorylation in response to insulin and NGF.
Subunit: Interacts with MORG1. Binds to HIV-1 Nef. This interaction inhibits its kinase activity. Interacts with HSF4 and NISCH. Also known as: Mitogen-activated protein kinase 3, Extracellular signal-regulated kinase 1, Insulin-stimulated MAP2 kinase, MAP kinase 1, MAPK 1, p44-ERK1, ERT2, p44-MAPK, Microtubule-associated protein 2 kinase, Mitogen-activated protein kinase 1, Extracellular signal-regulated kinase 2, ERK-2, Mitogen-activated protein kinase 2, MAP kinase 2, MAPK 2, p42-MAPK, ERT1, MAPK1, PRKM1, PRKM2, MAPK3, PRKM3.
Application Notes A concentration of 10-50 µg/ml is recommended.
The optimal concentration should be determined by the end user. This antibody may also recognise the unphosphorylated form.
Not yet tested in other applications.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
Expiry Date 12 months
Background publications Rikova, Guo, Zeng, Possemato, Yu, Haack, Nardone, Lee, Reeves, Li, Hu, Tan, Stokes, Sullivan, Mitchell, Wetzel, Macneill, Ren, Yuan, Bakalarski, Villen, Kornhauser, Smith, Li, Zhou, Gygi, Gu et al.: "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. ..." in: Cell, Vol. 131, Issue 6, pp. 1190-203, 2007 (PubMed).

Wissing, Jänsch, Nimtz, Dieterich, Hornberger, Kéri, Wehland, Daub: "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." in: Molecular & cellular proteomics : MCP, Vol. 6, Issue 3, pp. 537-47, 2007 (PubMed).

Olsen, Blagoev, Gnad, Macek, Kumar, Mortensen, Mann: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).

Zhang, Wolf-Yadlin, Ross, Pappin, Rush, Lauffenburger, White: "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." in: Molecular & cellular proteomics : MCP, Vol. 4, Issue 9, pp. 1240-50, 2005 (PubMed).

Charest, Mordret, Harder, Jirik, Pelech: "Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1." in: Molecular and cellular biology, Vol. 13, Issue 8, pp. 4679-90, 1993 (PubMed).

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