• Purity

  >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its ability to bind biotinylated 6’-Sialyllactose-Polyacrylamide in functional ELISA. Whitney, G.     et al. (2001) FEBS     268:6083. rhSiglec-10/Fc Chimera immobilized at 5 µg/mL (100 µL/well) on a goat anti-human IgG Fc antibody (Catalog # G-102-C) coated plate can bind biotinylated 6’-Sialyllactose-Polyacrylamide with a linear range of 0.04-2.5 µg/mL.

• Source

  Mouse myeloma cell line, NS0-derived

  Human Siglec-10 (Met17-Thr546) Accession # Q96LC7	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Met17

• Structure / Form

  Disulfide-linked heterodimer

• Predicted Molecular Mass

  85 kDa (monomer)

• SDS-PAGE

  105-110 kDa, reducing conditions

Background: Siglec-10

Siglecs (sialic acid binding Ig-like lectins) are I-type lectins that belong to the immunoglobulin superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by a varying number of Ig-like C2-type domains. Siglecs 5-11 constitute the CD33/Siglec-3 related group, and are differentially expressed in the hematopoietic system (1-3). Siglec-G is the apparent ortholog of human Siglec-10 (4). The human Siglec-10 cDNA encodes a 697 amino acid (aa) precursor that includes a 16 aa signal sequence, a 534 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 126 aa cytoplasmic domain. The ECD contains one Ig-like V-type domain and four Ig-like C2-type domains, while the cytoplasmic domain contains two immunoreceptor tyrosine-based inhibitory motifs (ITIM) (5-8). Five splice variants of human Siglec-10 differ in their deletions within the ECD. A potentially secreted sixth variant contains the Ig-like V-type domain followed by a 45 aa substitution (5-7, 9). Within the ECD, human Siglec-10 is most closely related to Siglec-5 (42% aa sequence identity). It shares 63% aa sequence identity with mouse Siglec-G. Siglec-10 is expressed on eosinophils, neutrophils, monocytes, and B cells (5, 8) with some splice variants predominating in particular cell types and tissue locations (6, 7, 9). It is upregulated on eosinophils in mouse models of allergic respiratory inflammation (10). Siglec-10 binds sialated proteins and lipids in alpha 2,3 or alpha 2,6 linkage and shows a preference for GT1b gangliosides (7, 11). This binding can be modulated by cis interactions of Siglec-10 with sialated molecules expressed on the same cell.(7) When tyrosine phosphorylated, the cytoplasmic ITIMs interact with phosphatases SHP-1 and SHP-2 to propagate inhibitory signals (5, 9).

• References:

1. Crocker, P.R. (2005) Curr. Opin. Pharmacol. 5:431.

2. Crocker, P.R. (2002) Curr. Opin. Struct. Biol. 12:609.

3. Crocker, P.R. and J. Zhang (2002) Biochem. Soc. Symp. 69:83.

4. Angata, T. et al. (2001) J. Biol. Chem. 276:45128.

5. Whitney, G. et al. (2001) Eur. J. Biochem. 268:6083.

6. Yousef, G.M. et al. (2001) Biochem. Biophys. Res. Commun. 284:900.

7. Li, N. et al. (2001) J. Biol. Chem. 276:28106.

8. Munday, J. et al. (2001) Biochem. J. 355:489.

9. Kitzig, F. et al. (2002) Biochem. Biophys. Res. Commun. 296:355.

10. Aizawa, H. et al. (2003) Genomics 82:521.

11. Rapoport, E. et al. (2003) Bioorg. Med. Chem. Lett. 13:675.

• Long Name:

  Sialic Acid Binding Ig-like Lectin 10

• Entrez Gene IDs:

  89790 (Human)

• Alternate Names:

  MGC126774; PRO940; sialic acid binding Ig-like lectin 10; sialic acid-binding Ig-like lectin 10; Siglec10; Siglec-10; siglec-like gene 2; Siglec-like protein 2; SLG2; SLG2sialic acid binding Ig-like lectin 10 Ig-like lectin 7