Sequence analysis predicted that the 335-amino acid transmembrane protein has a 225-residue extracellular domain, which has 7 putative N-linked glycosylation sites, and an 85-amino acid cytoplasmic domain, which contains 2 of the consensus tyrosine motifs and a third C-terminal tyrosine motif that has phe instead of thr.
Functional analysis indicated that CRACC mediates lysis that is in addition to that mediated by NKP46 or CD16. Further analysis determined that, unlike CD244, cytotoxicity mediated by CRACC or NKP46 is SAP-independent and that CRACC triggers ERK activation. Immunoblot analysis showed that CRACC is tyrosine phosphorylated in activated NK cells and is associated with 19- and 39-kD proteins.
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