Lck is a lymphoid-specific cytosolic protein tyrosine kinase (PTK), which is essential for T-cell development and function. It is constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors and plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, and thereby recruits the associated Lck to the vicinity of the TCR/CD3 complex. Lck then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAMs) in the cytoplasmic tails of the TCR-chains and CD3 subunits. The phospho-ITAMs serve as docking sites for Src homology domain 2 (SH2)-containing molecules, predominantly ZAP-70 and Syk. Only then can ZAP-70 undergo tyrosine phosphorylation, become enzymatically active and further phosphorylate downstream effector molecules. In addition, Lck contributes to signaling by other receptor molecules. Protein tyrosine kinase LCK is a non-receptor kinase belonging to the Src subfamily. LCK functions in a variety of ways, and therefore results in an assortment of diseases when not working properly. For example, T cell receptor binding activates LCK to induce downstream effects. In addition, LCK regulates chloride channel opening in lymphocytes. LCK is associated with various cancers and diseases, including neuroblastoma, Non-Hodgkins lymphoma, leukemia, SCID (severe combine immunodeficiency), and type I diabetes. Alternative splicing and differential promoter usage have been observed.
Immunogen
LCK monoclonal antibody was raised against a synthetic peptide containing amino acid residues of LCK (Human).
Key Feature
Clonality
Monoclonal
Isotype
IgG1
Host Species
Mouse
Tested Applications
IHCWB
LCK antibody can be used in ELISA, Western Blot starting at 1:500 - 1:1000, and immunohistochemistry starting at 10 - 20 μg/mL.: