|Other Names||Sialic acid-binding Ig-like lectin 11, Sialic acid-binding lectin 11, Siglec-11, SIGLEC11|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1630a was selected from the N-term region of human SIGLEC11 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,8- linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules.|
|Cellular Location||Membrane; Single-pass type I membrane protein|
|Tissue Location||Expressed by macrophages in various tissues including Kupffer cells. Also found in brain microglia|
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SIGLECs are a family of cell surface lectins defined by shared structural motifs in the first 2 immunoglobulin (Ig)-like domains and by their ability to recognize sialic acids via the first Ig V set domain. SIGLEC11 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha-2,8-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, this protein may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules.
Clark, H.F., et al., Genome Res. 13(10):2265-2270 (2003).Angata, T., et al., J. Biol. Chem. 277(27):24466-24474 (2002).
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