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AFP can be fractionated by affinity electrophoresis into three glycoforms: L1, L2, and L3 based on the reactivity with the lectin Lens culinaris agglutinin (LCA). AFP-L3 binds strongly to LCA via an additional α 1-6 fucose residue attached at the reducing terminus of N-acetylglucosamine; this is in contrast to the L1 isoform.
Having a super-sensitive multi-cancer screening tool that could actually save lives is the ... For about 1% of those ages 50 to 79, test results will show a cancer signal was detected, along with ...
A lectin from Ulex europaeus is used to identify the H blood group antigen. A lectin from Vicia graminea is used to identify the N blood group antigen. A lectin from Iberis amara is used to identify the M blood group antigen. Non blood-group antigens can be identified by lectins: A lectin from coconut milk is used to identify Theros antigen.
A C-type lectin (CLEC) is a type of carbohydrate-binding protein known as a lectin. [3] The C-type designation is from their requirement for calcium for binding. [4] Proteins that contain C-type lectin domains have a diverse range of functions including cell-cell adhesion, immune response to pathogens and apoptosis.
C-type lectin domain family 10 member A (CLEC10A) also designated as CD301 is a protein that in humans is encoded by the CLEC10A gene. [5] CLEC10A is part of the C-type lectin superfamily and binds to N-Acetylgalactosamine (GalNAc). It is mainly expressed on myeloid cells and also on oocytes and very early stages of embryogenesis.
L-selectin is composed of multiple structural regions: an N-terminus C-type lectin domain, an adjacent epidermal growth factor-like domain, two to the consensus repeat units homologous to those found in C3/C4-binding proteins, an extracellular cleavage site, a short transmembrane domain, and a cytoplasmic tail.