SIGLEC9 (sialic acid binding Ig-like lectin 9) gene encodes a member of the Siglec (sialic acid-binding Ig-like lectin) family that belongs to the immunoglobulin superfamily (IgSF). Siglecs are type-I transmembrane proteins that are expressed mainly on immune cells. The gene SIGLEC9 consists of seven exons interspaced by six introns and is mapped to human chromosome 19q13.4. The encoded protein spans a length of 463-amino-acids. Siglec-9 has been found to be expressed abundantly in bone marrow, placenta, spleen, and fetal liver. The Siglec family is characterized by the presence of one N-terminal V-set domain and a variable number of downstream C2 set domains. The members of this family are involved in mediating protein-carbohydrate interactions via specific interactions with sialic acid-containing glycoproteins and glycolipids.
Synonyms: Anti-Protein FOAP-9; Anti-Sialic acid-binding Ig-like lectin 9 precursor; Anti-Siglec-9
MDL Number: MFCD03455968
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: Siglec-9 is a lectin that binds to sialic acids via the N-terminal V-set Ig domain. It contains tyrosine-based inhibitory motifs in its cytoplasmic tail. It inhibits unwanted neutrophil reactivity and controls innate immune response by recognizing host sialic acids as 'self'. It binds preferentially to a-2,3- or a-2,6-linked sialic acid. It facilitates the transduction of apoptotic and nonapoptotic death signals into neutrophils.
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