Recombinant human MK2 / MAPKAPK2, protein kinase,10 µg

Background: Mitogen-activated protein kinase (MAPK)-activated protein kinase 2 (MK2) belongs to the calcium/calmodulin-dependent protein-kinase (CaMK) group of MAPKAPK, represented by MAPKAPK2 / MK2, MAPKAPK3 / MK3 and MAPKAPK5 / MK5 that function downstream of mitogen-activated protein kinases (MAPKs). Protein structure consists of an N-terminal proline-rich region, a catalytic domain and a nuclear localization sequence (NLS) and the nuclear export sequence (NES) at the C-termini. MAPKAPK2 / MK2 is activated by phosphorylation by MAPK p38. MK2/3–p38 α complex exists in the nucleus. In this conformation, the MK2/3 nuclear localization signal (NLS) is functional whereas the nuclear export signal (NES) is masked. After stress stimulation, MAPK kinase-6 (MKK6) phosphorylates and activates p38 α, which, in turn, phosphorylates and activates MK2/3 in the nuclear complex. During the activation of MK2/3, the NES is exposed and the complex of active p38 α and MK2/3 is actively exported from the nucleus.

Human MAPKAPK2 (MAP kinase activated protein kinase 2), untagged, recombinant and active enzyme, activated, untagged, ecpressed in insect cells

Theoretical MW : 42.329 kDa (fusion proteins)
Expression system: Baculovirus infected Sf9 cells
Purification: Immobilized Metal Affinity Chromatography
Storage buffer: 50 mM HEPES pH 7.5, 100 mM NaCl, 5 mM DTT, 20% glycerol
Protein concentration: 0.340 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MSFC membrane
Specific activity : 101,000 pmol/mg mi

Entrez Gene ID: 9261
UniProtKB: P49137

Ordering information: shipped on dry ice

Product specific literature:

Gaestel M. (2006) "MAPKAP kinases - MKs - two's company, three's a crowd."Nat Rev Mol Cell Biol. 7(2):120-30.

Shiryaev A1, Dumitriu G, Moens U. (2011) "Distinct roles of MK2 and MK5 in cAMP/PKA- and stress/p38MAPK-induced heat shock protein 27 phosphorylation."J Mol Signal. 2011 May 16;6(1):4. doi: 10.1186/1750-2187-6-4.