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KMID : 0357119960180010065
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Korean Journal of Immunology
1996 Volume.18 No. 1 p.65 ~ p.74
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production of Recombinant Human Grb2 SH2 Fusion Protein and It's Antibody
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윤선영
이경미/김재화/권병목/최인성/한미영
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Abstract
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Binding of SH2 domains to tyrosine-phosphorylated regions of growth factor receptors is though to provide a common mechanism by which diverse regulatory proteins can interact specifically with activated growth factor receptors and thereby
transduce
activated receptor signal to multiple intracellular signalling pathway. Therefore, many researchers have been trying to elucidate the roles and to design of binding assay for the SH2 domain of signal transducer(Grb2, PLCγ-1, PI-3K p85). The SH2
domain
of Grb2 binds to the carboxy -terminal tail of activated EGFR or Shc protein via interactions with an autophosphorylated tyrosine residue and then implicated to Ras pathway. To understand the another roles of Grb2 SH2 protein as an adaptor
protein
in
signal transduction pathway, convenient source for recombinant Grb SH2 protein and anti-Grb2 SH2 antibodies are necessary. Therefore, we cloned Grb2 SH2 domain from Grb2 cDNA clone by DNA Polymerase chain reaction. And Grb2 SH2 expression vector
was
constructed and produced of recombinant Grb2 SH2 protein. We also produced polyclonal antibodies against Grb2 SH2 recombinant proteins and conformed the specificity of the antibodies.
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