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Mutation of the basic clusters in the CD28 (zeige CD28 Proteine) cytoplasmic domain reduced the recruitment to the CD28 (zeige CD28 Proteine)-Lck complex of protein kinase (zeige CDK7 Proteine) Ctheta; (PKCtheta (zeige PRKCQ Proteine);), which serves as a key effector kinase in the CD28 (zeige CD28 Proteine) signaling pathway.
A phosphosite within the SH2 Domain of Lck regulates its activation by CD45. A negative feedback loop that responds to signaling events tunes active Lck amounts and TCR sensitivity.
We show a striking 65% reduction in cellularity, preferential development of gammadelta versus alphabeta T cells, and increased expression of IL-7R in the thymus of mice expressing Cre under the proximal lck promoter (lck-cre(+) mice)
this work demonstrates a role for constitutive Lck activity in controlling antigen sensitivity
this study defines distinct and complementary requirements for proximal and distal lck promoters during T-cell development
Aurora A (zeige AURKA Proteine) inhibition causes delocalized clustering of Lck at the immunological synapses and decreases its phosphorylation levels thus indicating Aurora A (zeige AURKA Proteine) is required for maintaining Lck active during T-cell activation.
essential for thymic development in presence or absence of Cbl, ensuring MHC restriction of T cells
Lck-Dlx5 (zeige DLX5 Proteine) mice develop T-ALLs that consistently acquire overexpression of Myc (zeige MYC Proteine) and activation of Akt (zeige AKT1 Proteine).
Lck-CD8 (zeige CD8A Proteine) interaction is required for initial CD8 (zeige CD8A Proteine) recruitment.
The kinase Itk (zeige ITK Proteine) and the adaptor TSAd (zeige SH2D2A Proteine) change the specificity of the kinase Lck in T cells by promoting the phosphorylation of Tyr192.
The ionic CD3-epsilon (zeige CD3E Proteine) -Lck interaction controls the phosphorylation level of the T-cell receptor.
a previously unappreciated role for PLC-gamma1 (zeige PLCG1 Proteine) in the positive regulation of Zap-70 (zeige ZAP70 Proteine) and T-cell receptor tyrosine phosphorylation. Conversely, PLC-gamma1 (zeige PLCG1 Proteine) negatively regulated the phosphorylation of SLP-76 (zeige LCP2 Proteine)-associated proteins, including previously established Lck substrate phosphorylation sites within this complex.
autophosphorylation of the LCK active-site loop is indispensable for its catalytic activity and LCK can stimulate its own activation by adopting a more open conformation, which can be modulated by point mutations, and CD4 (zeige CD4 Proteine) and CD8 (zeige CD8A Proteine), T-cell coreceptors, can enhance LCK activity
the central biological role of the novel IL-2 (zeige IL2 Proteine)-R/Lck/PLCgamma/PKCtheta (zeige PRKCQ Proteine);/alphaPIX (zeige ARHGEF6 Proteine)/Rac1/PYGM (zeige PYGM Proteine) signalling pathway is directly related to the control of fundamental cellular processes such as T cell migration and proliferation.
Possible models of regulation of Lck by Aurora-A (zeige AURKA Proteine) during T cell activation are described in the review.
Data suggest that T cell activation through the TCR complex is accompanied by the de novo activation of T-lymphocyte specific protein tyrosine kinase p56lck (Lck) and that phosphorylation of Tyr (zeige TYR Proteine)(394) plays a role in Lck function that goes beyond inducing an open conformation of the kinase.
WASH has a pivotal role for regulation of NK cell cytotoxicity through Lck-mediated Y141 tyrosine phosphorylation.
The results have revealed a novel splicing homozygous mutation of LCK that may be responsible for the clinical phenotype of HPV infection from latency to invasive carcinoma.
LCK gene could be an useful candidate gene in selection for increasing litter size in pigs.
This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded 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. Multiple alternatively spliced variants, encoding the same protein, have been described.
lymphocyte protein tyrosine kinase
, lymphocyte-specific protein tyrosine kinase
, tyrosine-protein kinase Lck-like
, leukocyte C-terminal Src kinase
, lymphocyte cell-specific protein-tyrosine kinase
, proto-oncogene tyrosine-protein kinase LCK
, T-lymphocyte specific protein tyrosine kinase p56lck
, p56(LSTRA) protein-tyrosine kinase
, t cell-specific protein-tyrosine kinase
, tyrosine-protein kinase Lck
, tyrosine protein kinase
, tyrosine-protein kinase LCK