- Phosphorylation and activation of the Jak-3 Janus kinase in response to interleukin-2.
Phosphorylation and activation of the Jak-3 Janus kinase in response to interleukin-2.
Nature (1994-07-14)
J A Johnston, M Kawamura, R A Kirken, Y Q Chen, T B Blake, K Shibuya, J R Ortaldo, D W McVicar, J J O'Shea
PMID8022485
RESUMEN
Interleukin-2 is an autocrine growth factor for T cells which also activates other cells including B cells and natural killer cells. The subunits of the interleukin-2 receptor (IL-2R) lack intrinsic enzymatic activity, but protein tyrosine phosphorylation is a critical event following ligand binding and src family kinases, such as Lck, are known to be activated by IL-2 (refs 5-9). However, IL-2 signalling can occur in the absence of receptor interaction with Lck, suggesting that other protein tyrosine kinases might be important. Here we report that a new member of the Janus family of kinases (Jak-3) is coupled to the IL-2R in human peripheral blood T cells and natural killer cells.
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JAK3 Protein, active, 10 µg, Active, N-terminal His6-tagged, recombinant, human JAK3 amino acids 781-end, for use in Kinase Assays.