In a functional ELISA. Recombinant Mouse Siglec-G Fc Chimera (Catalog # 10103-SL) binds to biotinylated 6'-Sialylactose-PAA.
2 μg/lane of Recombinant Mouse Siglec-G Fc Chimera(Catalog # 10103-SL) was resolved with SDS-PAGE under reducing (R) andnon-reducing (NR) conditions and visualized by Coomassie®Blue staining, showing bands at ...read more
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
86 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
102-114 kDa, under reducing conditions
Publications
Read Publication using 10103-SL in the following applications:
Siglecs
are type I transmembrane proteins that belong to the immunoglobulin (Ig)
superfamily and function as mammalian lectins (1). They are characterized by an extracellular
domain consisting of various numbers of Ig domains with a conserved N-terminal
V-set Ig ligand-binding domain. This binds species-specific sialic acid motifs
on protein and lipid scaffolds to regulate intracellular signaling pathways (2).
The cytoplasmic tail has signaling motifs, in most cases immunoreceptor
tyrosine-based inhibitory motif (ITIM) (3). Siglec-G is a member of the CD33-related
Siglec family in the mouse. It
is the apparent ortholog of human Siglec-10 (4). It is expressed by mature B cells, but
significant levels of transcript were also detected in DC, myeloid cells, and
to a lesser extent, T cells (5). Mature Siglec-G
consists of a 526 amino acid (aa) extracellular domain (ECD), a 21 aa
transmembrane segment, and a 124 aa cytoplasmic domain. Within the ECD, mouse
Siglec-G shares 63% and 86% aa sequence identity with the human and rat
ortholog Siglec-10, respectively. Siglec-10 binds sialated proteins and lipids in
alpha 2,3 or alpha 2,6 linkage and shows a preference for GT1b gangliosides
(6, 7). This binding can be modulated by cis interactions of Siglec-10 with
sialated molecules expressed on the same cell (6). When tyrosine
phosphorylated, the cytoplasmic ITIMs interact with phosphatases SHP-1 and
SHP-2 to propagate inhibitory signals (8, 9).
Crocker, P.R. et al. (2007) Nat. Rev. Immunol. 7:255.
Poe, J.C. and T.F. Tedder (2012) Trends Immunol. 33:413.
Meyer, S.J. et al. (2018) Front. Immunol. 9:2820.
Angata, T. et al. (2001) J. Biol. Chem. 276:45128.
Chen, G-Y, et al. (2014) Glycobiology 24:800.
Li, N. et al. (2001) J. Biol. Chem. 276:28106
Rapoport, E. et al. (2003) Bioorg. Med. Chem. Lett. 13:675.
Whitney, G. et al. (2001) Eur. J. Biochem. 268:6083.
Kitzig, F. et al. (2002) Biochem. Biophys. Res. Commun. 296:355.
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