Anti-Mouse/Human GL7 - FITC (G222-GRP)

GL7 antibody was originally used in mouse to identify a 35 kDa cell surface protein expressed selectively on subpopulations of activated B and T cells as well as discrete subpopulations of T and B lineage cells in vivo 1GL7 antibody was originally used in mouse to identify a 35 kDa cell surface protein expressed selectively on subpopulations of activated B and T cells as well as discrete subpopulations of T and B lineage cells in vivo1. GL7 recognizes a glycan moiety containing a terminal sialic acid (Sia)2. Determinant recognition by GL7 is specific to Neu5Ac-bearing glycans, which is a Sia modification at the C-5 position. GL7 reactivity has been assessed against various mouse and human B cell lines2. In mouse bone marrow, GL7 first appears on the cell surface of B220+CD117+ pro-B cells and then peaks at the B220+CD40- pro-B/pre-B-I transition, with expression decreasing slightly after the pre-B-I phase3,4. GL7 expression remains high on pre-B-II and immature B cells but is almost completely downregulated on mature B cells3. This phenotype is independent of mouse genetic background. In contrast, thymic GL7 expression differs between BALB/c and C57BL/6 strains5. GL7 has stronger reactivity against human B cell lines than mouse B cell lines2. Staining patterns show that the GL7 epitope on Daudi cells is similar to that of mouse activated B cells and is inhibited by broad sialidase treatment but not treatment specific to α2,3-linked Sia. Differences in GL7 epitope expression, caused by differential expression of enzymes involved in the biosynthesis of the GL7 epitope glycan, rather than differences in carrier protein expression, leads to variable staining in human B cell lines. ST6GAL1 has the strongest correlation with the GL7 staining profile.