Phospho-LCK (Tyr505) Recombinant antibody

Lck is comprised of a SH3 domain, binding prolinerich regions, a SH2 domain, binding tyrosine-phosphorylated sequences, a kinase domain, a unique domain, and the negative regulatory tail. The kinase domain of Lck contains 2 important tyrosine residues. Tyr394 and Tyr505 represent the activating and inhibitory tyrosine residue, respectively. Therefore, Lck can exist in 4 distinct states of activity: an inactive state, a primed state, an active state, and a dually phosphorylated active state . Transitions between activity states are governed by phosphorylation at the Tyr394 and Tyr505 residues. When Tyr394 is dephosphorylated while Tyr505 is phosphorylated, Lck is in an inactive state. Lck becomes primed when Tyr505 is dephosphorylated and fully active after Tyr394 phosphorylation. In addition, there is a dually phosphorylated active form of Lck when both Tyr394 and Tyr505 residues are phosphorylated. (PMID: 32794043)