|Other Names||Sialic acid-binding Ig-like lectin 12, Siglec-12, Sialic acid-binding Ig-like lectin-like 1, Siglec-L1, SIGLEC12, SIGLECL1, SLG|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1634b was selected from the C-term region of human SIGLEC12. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI 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. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.|
|Cellular Location||Membrane; Single-pass type I membrane protein|
|Tissue Location||Isoform Short is highly expressed in spleen, small intestine and adrenal gland; it is lower expressed in thyroid, placenta, brain, stomach, bone marrow, spinal chord and breast. Isoform Long is highly expressed in spleen, small intestine and bone marrow; it is lower expressed in thyroid, placenta, thymus, trachea, stomach, lung, adrenal gland, fetal brain and testis|
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Provided below are standard protocols that you may find useful for product applications.
Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. SIGLEC12 is a member of the SIGLEC3-like subfamily of SIGLECs. Members of this subfamily are characterized by an extracellular V-set immunoglobulin-like domain followed by two C2-set immunoglobulin-like domains, and the cytoplasmic tyrosine-based motifs ITIM and SLAM-like. This protein, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor.
Angata,T., J. Biol. Chem. 276 (43), 40282-40287 (2001)Yu,Z., J. Biol. Chem. 276 (26), 23816-23824 (2001)Foussias,G., Biochem. Biophys. Res. Commun. 284 (4), 887-899 (2001)
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