CD367/CLEC4A Protein, Mouse (Myc, His-SUMO)

CD367/CLEC4A protein may regulate immune responses and affect dendritic cell (DC) differentiation. As a C-type lectin receptor, it binds carbohydrates and interacts weakly with N-acetylglucosamine. CD367/CLEC4A Protein, Mouse (Myc, His-SUMO) is the recombinant mouse-derived CD367/CLEC4A protein, expressed by E. coli , with N-His, C-Myc, N-SUMO labeled tag. The total length of CD367/CLEC4A Protein, Mouse (Myc, His-SUMO) is 169 a.a., with molecular weight of ~39.6 kDa.

The CD367/CLEC4A protein potentially plays a role in regulating immune reactivity and may have implications in modulating the differentiation and maturation of dendritic cells (DC). It is a C-type lectin receptor that can bind to carbohydrates such as mannose and fucose, as well as weakly interact with N-acetylglucosamine (GlcNAc) in a Ca(2+)-dependent manner. CD367/CLEC4A is involved in inhibiting B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation. Upon antigen stimulation, it undergoes clathrin-dependent endocytosis, delivering its antigenic cargo into the antigen presentation pathway and promoting cross-priming of CD8(+) T cells. This cross-presentation and cross-priming process can be enhanced by TLR7 and TLR8 agonists, resulting in increased expansion of CD8(+) T cells and high production of IFNG and TNF, while reducing levels of IL4, IL5, and IL13. In plasmacytoid dendritic cells, CD367/CLEC4A inhibits TLR9-mediated production of IFNA and TNF. Furthermore, its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) may contribute to the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation.

Mouse

E. coli

N-His;C-Myc;N-SUMO

Q9QZ15 (70Q-238L)

26888  [NCBI]

QKYSQLLEEKKAAKNIMHNELNCTKSVSPMEDKVWSCCPKDWRLFGSHCYLVPTVSSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGILDTHAAYFIGLWDTGHRQWQWVDQTPYEESITFWHNGEPSSGNEKCATIIYRWKTGWGWNDISCSLKQKSVCQMKKINL

Approximately 39.6 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.