Phospho-DUSP1/MKP1 (Ser359) (125E2) Rabbit mAb #2857
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 40 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Phospho-DUSP1/MKP1 (Ser359) (125E2) Rabbit mAb detects endogenous levels of DUSP1 only when phosphorylated at serine 359.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser359 of human DUSP1.
Background
MAP kinases are inactivated by a family of dual-specificity protein phosphatases (DUSP) that differ in their substrate specificity, tissue distribution, inducibility by extracellular stimuli and cellular localization. DUSP1/MKP1 (MAP Kinase phosphatase 1) is primarily localized in the nucleus, and has broad substrate specificity towards p44/42 MAPK, p38 MAPK and SAPK/JNK (1-3). DUSP1's transcription and activity are tightly regulated. First, DUSP1 is transcriptionally induced through p44/42 MAPK, p53 and Jak2 (2,4,5). Second, DUSP1 is phosphorylated by p44/42 MAPK at Ser359 and Ser364 in its carboxy-terminal region, which inhibits DUSP1 degradation through the ubiquitin pathway (6).
- Sun, H. et al. (1993) Cell 75, 487-93.
- Brondello, J.M. et al. (1997) J Biol Chem 272, 1368-76.
- Franklin, C.C. and Kraft, A.S. (1997) J Biol Chem 272, 16917-23.
- Li, M. et al. (2003) J Biol Chem 278, 41059-68.
- Sandberg, E.M. et al. (2004) J Biol Chem 279, 1956-67.
- Brondello, J.M. et al. (1999) Science 286, 2514-7.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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