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Background: DDR2 is a receptor tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. By up-regulation of the collagenases MMP1, MMP2 and MMP13 DDr2 regulates remodeling of the extracellular matrix and thereby facilitates cell migration and tumor cell invasion.
Human discoidin domain receptor family, member 2, C-terminal fragment,amino acids R422-E855 (kinase domain), recombinant and active enzyme, N-terminal GST-HIS6 fusion protein with a 3C cleavage site, expressed in Sf9 insect cells
Theoretical MW: 77.801 kDa (fusion protein)
Expression system: Baculovirus infected Sf9 cells
Purification: GST-Affinity Chromatography
Storage buffer: 50 mM HEPES pH 7.5, 100 mM NaCl, 5 mM DTT, 15 mM reduced glutathione, 20% glycerol
Protein concentration: 0.102 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MSFC membrane
Specific activity: 89,000 pmol/mg x min
Entrez Gene ID: 4921
UniProtKB: Q16832
Ordering information: shipped on dry ice
Vogel W., Gish G.D., Alves F., Pawson T.(1997) "The discoidin domain receptor tyrosine kinases are activated by collagen." Mol. Cell 1:13-23
Wall S.J., Werner E., Werb Z., DeClerck Y.A. (2005) "Discoidin domain receptor 2 mediates tumor cell cycle arrest induced by fibrillar collagen."J. Biol. Chem. 280:40187-40194
Vogel W.F., Abdulhussein R., Ford C.E.(2006)"Sensing extracellular matrix: an update on discoidin domain receptor function."Cell. Signal. 18:1108-1116
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