|Other Names||Sialoadhesin, Sialic acid-binding Ig-like lectin 1, Siglec-1, CD169, SIGLEC1, SN|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1621b was selected from the C-term region of human SIGLEC1 . 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||Acts as an endocytic receptor mediating clathrin dependent endocytosis. Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Preferentially binds to alpha-2,3-linked sialic acid (By similarity). Binds to SPN/CD43 on T-cells (By similarity). May play a role in hemopoiesis.|
|Cellular Location||Isoform 1: Cell membrane; Single-pass type I membrane protein|
|Tissue Location||Expressed by macrophages in various tissues. High levels are found in spleen, lymph node, perivascular macrophages in brain and lower levels in bone marrow, liver Kupffer cells and lamina propria of colon and lung. Also expressed by inflammatory macrophages in rheumatoid arthritis|
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Provided below are standard protocols that you may find useful for product applications.
SIGLEC1, encoded by a immunoglobulin superfamily gene, is a lectin-like adhesion molecule which binds glycoconjugate ligands on cell surfaces in a sialic acid-dependent manner. It is a type I transmembrane protein expressed only by a subpopulation of macrophages and is involved in mediating cell-cell interactions. Alternative splicing of the gene produces a variant encoding a protein isoform that is soluble rather than membrane-bound; however, the full-length nature of this variant has not been determined.
Hartnell, A., et al., Blood 97(1):288-296 (2001).Nath, D., et al., Immunology 98(2):213-219 (1999).Mucklow, S., et al., Genomics 28(2):344-346 (1995).
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