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TRIM required LAX for binding to Rab8 in a complex, a novel CTLA-4/TRIM/LAX/Rab8 effector complex in the transport of CTLA-4 to the surfaces of T cells
We identified the transmembrane domain of LAX as a first motif targeting transmembrane protein constructs to detergent-resistant heavy rafts, a novel type of membrane microdomains containing a number of physiologically important proteins.
Overexpression of LAX in Jurkat cells specifically inhibits T cell receptor-mediated p38 MAPK activation and NFAT/AP-1 transcriptional activation.
inhibition of signaling events involved in T cell activation by LAX occurs through mechanisms both dependent on and independent of its tyrosine phosphorylation.
SIT and LAX are important negative regulators of immune responses that functionally cooperate.
Upon T or B cell activation, the LAX protein is up-regulated dramatically. This in vivo study of LAX-deficient mice demonstrates that LAX functions as a negative regulator in lymphocyte signaling.
LAX negatively regulates mast cell function
Negatively regulates TCR (T-cell antigen receptor)- mediated signaling in T-cells and BCR (B-cell antigen receptor)- mediated signaling in B-cells (By similarity).
lymphocyte transmembrane adaptor 1
, lymphocyte transmembrane adapter 1-like
, LAT-like membrane associated protein
, linker for activation of x cells
, lymphocyte transmembrane adapter 1
, membrane-associated adapter protein LAX
, membrane associated adaptor protein LAX
, linker for activation of X cells