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Our results provide new insight into the effect of ITK and suboptimal T-cell receptor signaling on CD8 (show CD8A Proteins)(+) T cell function, and how these may contribute to phenotypes associated with ITK deficiency
Data suggest that the pleckstrin homology domain of Itk functions as a phospholipid bilayer recognition site that localizes Itk to membrane via phosphatidylinositol 3,4,5-trisphosphate (PIP3) binding; this specific binding inhibits the phospho-transfer reaction via an allosteric mechanism.
pharmacological inhibition of ITK resulted in T cell hyperplasia and the increased production of TH2-type cytokines.
ITK and BTK (show BTK Proteins) regulate thermal homeostasis during septic response through mast cell function in mice.
Taken together, these data indicate that ITK plus RLK (show TXK Proteins) inhibition may have therapeutic potential in Th1 (show HAND1 Proteins)-mediated inflammatory diseases.
This work has important implications for understanding the role of Itk signaling in the development versus function of iNKT cells, Th1 (show HAND1 Proteins), Th2, and Th17 cells.
The kinase Itk and the adaptor TSAd (show SH2D2A Proteins) change the specificity of the kinase Lck (show LCK Proteins) in T cells by promoting the phosphorylation of Tyr192.
Data indicate that the interleukin-2 (show IL2 Proteins) inducible tyrosine kinase (show TYRO3 Proteins) K390R point mutation (Itk-KD) transgenic mice were largely protected from inflammatory symptoms in an Ovalbumin (show OVA Proteins) model of airway inflammation.
The Itk pleckstrin (show PLEK Proteins) homology domain binds to Calmodulin and PI(3,4,5)Pto promote efficient calcium signaling and IL-17A (show IL17A Proteins) production.
Signaling by Itk promotes autoimmunity and CNS inflammation.
The data indicate that increased ITK expression could act as a disease activity marker and as a risk factor for involvement in SLE, but it still needs further study to confirm.
We conclude that ITK, formerly considered an immune cell-specific protein, is aberrantly expressed in melanoma and promotes tumor development and progression
Found that 38% and 14% of the Angioimmunoblastic T-cell lymphoma cases exhibited gains of ITK and SYK (show SYK Proteins) genes, respectively.
These data indicate that PRN694 is a highly selective and potent covalent inhibitor of ITK and RLK (show TXK Proteins), and its extended target residence time enables durable attenuation of effector cells in vitro and in vivo.
approach identified 18 kinase and kinase-related genes whose overexpression can substitute for EGFR (show EGFR Proteins) in EGFR (show EGFR Proteins)-dependent PC9 (show PCSK9 Proteins) cells, and these genes include seven of nine Src (show SRC Proteins) family kinase genes, FGFR1 (show FGFR1 Proteins), FGFR2 (show FGFR2 Proteins), ITK, NTRK1 (show NTRK1 Proteins), NTRK2 (show NTRK2 Proteins), MOS (show MOS Proteins), MST1R (show MST1R Proteins), and RAF1 (show RAF1 Proteins).
ITK deficiency is a genetic cause of idiopathic CD4 (show CD4 Proteins)+ T-cell lymphopenia.
Data indicate reduced T-cell activation by altered IL-2 inducible T-cell kinase (ITK) expression in vitro.
T-cell-specific human ITK-Syk (show SYK Proteins) oncogene (show RAB1A Proteins) in mice leads to early polyclonal T cell lymphoproliferation (show FAS Proteins) with B cell expansion. It induces terminal T cell differentiation via Blimp-1 (show PRDM1 Proteins), eliminating oncogene (show RAB1A Proteins)-expressing cells early in development.
This gene encodes an intracellular tyrosine kinase expressed in T-cells. The protein contains both SH2 and SH3 domains which are often found in intracellular kinases. It is thought to play a role in T-cell proliferation and differentiation.
, interleukin-2-inducible T cell kinase
, kinase TLK
, tyrosine-protein kinase ITK/TSK
, IL-2-inducible T cell kinase
, IL-2-inducible T-cell kinase
, homolog of mouse T-cell itk/tsk
, interleukin-2-inducible T-cell kinase
, kinase EMT
, tyrosine-protein kinase LYK