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Phosphorylation and dephosphorylation of cellular proteins are central steps in transducing extracellular signals to the cell nucleus. Phosphorylated epitopes may serve as docking sites for the assembly of protein complexes or may alter the 3-dimensional protein structure thus modulating enzymatic activity or the ability to undergo protein-protein interactions.
Modification of proteins on serine residues is mediated by serine/threonine kinases.
Tyrosine residues are modified by protein tyrosine kinases. Tyrosine phosphorylation may alter the biological activity or mediate the assembly of protein complexes via the interaction of phosphotyrosine residues with SH2 or PID domains.

Monoclonal antibodies against:

Phosphoserine
Phosphotyrosine
Phosphothreonine

also availble as:

Phosphoserine, -tyrosine or -threonine Detection Kit

For further product information please click here


Please see also our phosphorylation-site specific monoclonal antibodies:

EGFR/erbB phosphorylation-sites

Akt signalling phosphorylation-sites

beta-Catenin phosphorylation-sites

MAP-/SAP kinases phosphorylation-sites

Receptor tyrosine kinases phosphorylation-sites

Tyrosine kinases phosphorylation-sites

Serine-Threonine kinases phosphorylations-sites



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