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:
also available as:
Phosphoserine, -tyrosine or -threonine Detection Kit
Please see also our phosphorylation-site specific monoclonal antibodies:
Akt signalling phosphorylation-sites
MAP-/SAP kinases phosphorylation-sites
Receptor tyrosine kinases phosphorylation-sites
Tyrosine kinases phosphorylation-sites
Serine-Threonine kinases phosphorylations-sites
See also: Phosphospecific and Modification State Specific Antibodies
All phosphospecific Antibodies from nanoTools