|Application ||IHC-P, WB, E|
|Calculated MW||64984 Da|
|Antigen Region||565-595 aa|
|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||This SIGLEC12 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 565-595 amino acids from the C-terminal region of human SIGLEC12.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SIGLEC12 Antibody (C-term) is for research use only and 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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