Lck Protein Schematic–Lck is a 56 kDa, membrane-associated, non-receptor tyrosine kinase belonging to the Src family that plays a critical role in T-cell antigen receptor (TCR) signaling, inducing T-lymphocyte development, activation, proliferation and survival. Lck has been implicated in various diseases including cancer development and metastasis, viral infections relating to HIV, heart disease, and osteoclast-mediated bone resorption. Lck is regulated by phosphorylation on multiple residues including Ser-194 in the SH2 domain, Tyr-394 (autophosphorylation site) within the activation loop of the catalytic domain, and Tyr-505 (inhibitory site) near the C-terminus. TCR requires Lck for thymocyte differentiation and activation. Additionally, Lck is implicated in JAK and STAT signaling, which are constitutively activated in cells overexpressing Lck.
|Tested species reactivity||Human|
|Published species reactivity||Not Applicable|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phosphopeptide from human Lck containing tyrosine 505 (based on Swiss Protein database, accession number P06239). The sequence is conserved in mouse.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3, with 50% glycerol, 1mg/ml BSA|
|Contains||0.05% sodium azide|
|Tested Applications||Dilution *|
|Western Blot (WB)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Miscellaneous PubMed (MISC)||See 1 publications below|
LCK is a member of the Src family of protein tyrosine kinases (PTKs). This protein is a key signaling molecule in the selection and maturation of developing T-cells. It contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to the plasma membrane and pericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and other signaling molecules.
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A reverse-phase protein microarray-based screen identifies host signaling dynamics upon Burkholderia spp. infection.
44-850G was used to identify host signaling dynamics upon Burkholderia spp. infection by a reverse-phase protein microarray-based screen
|Chiang CY,Uzoma I,Lane DJ,Memi¿evi¿ V,Alem F,Yao K,Kota KP,Bavari S,Wallqvist A,Hakami RM,Panchal RG||Frontiers in microbiology (6:null)||2015|