Siglec-8, also known as SAF, is an approximately 75 kDa transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules. Mature human Siglec-8 consists of a 347 amino acid (aa) extracellular domain (ECD) with three Ig-like domains.Putative adhesion molecule that mediates sialic-acid dependent binding to red blood cells. Preferentially binds to alpha-2,3-linked sialic acid. Also binds to alpha-2,6-linked sialic acid. Siglec-8 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 40.7 kDa and the accession number is Q9NYZ4.

Siglec-8 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with C-6xHis tag. The predicted molecular weight is 40-60 KDa and the accession number is Q9NYZ4.

Siglec-8 is also known as SIGLEC8, SAF2, SIGLEC-8, SIGLEC8L and sialic acid binding Ig like lectin 8, is an approximately 75 kDa transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules. Siglec-8 is expressed on eosinophils, basophils, and mast cells, and it shows a binding preference for the carbohydrate 6-O sulfated sLex. At the tissue level, Siglec-8 mRNA was found to be most highly expressed in lung, PBMCs, spleen, and kidney. Mature human Siglec-8 consists of a 347 amino acid (aa) extracellular domain (ECD) with three Ig-like domains, a 21 aa transmembrane segment, and a 115 aa cytoplasmic domain with two tyrosine based signaling motifs. Alternative splicing generates additional isoforms that either lack most of the second Ig-like domain or have a substituted cytoplasmic domain without the signaling motifs. Cross-linking of Siglec-8 inhibits Fc epsilon RI alpha induced mast cell degranulation. It also induces eosinophil apoptosis, an effect which is enhanced by the eosinophil-activating cytokines IL-5, IL-33, and GM-CSF.

Siglec-8, also known as SAF, is an approximately 75 kDa transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules. Mature human Siglec-8 consists of a 347 amino acid (aa) extracellular domain (ECD) with three Ig-like domains.Putative adhesion molecule that mediates sialic-acid dependent binding to red blood cells. Preferentially binds to alpha-2,3-linked sialic acid. Also binds to alpha-2,6-linked sialic acid. Siglec-8 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 40.7 kDa and the accession number is Q9NYZ4.

Siglec-8 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-Fc tag. The predicted molecular weight is 80-100 KDa and the accession number is Q9NYZ4.

Siglec 5 to 11 share a high degree of sequence similarity with CD33/Siglec-3 both in their extracellular and intracellular regions. They are collectively referred to as CD33-related Siglecs. One remarkable feature of the CD33-related Siglecs is their differential expression pattern within the hematopoietic system. This fact, together with the presence of two conserved immunoreceptor tyrosine-based inhibition motifs (ITIMs) in their cytoplasmic tails, suggests that CD33-related Siglecs are involved in the regulation of cellular activation within the immune system. Mouse Siglec-F cDNA encodes a 569 amino acid polypeptide with a hydrophobic signal peptide, an N-terminal Ig-like V-type domain, three Ig-like C2-type domains, a transmembrane region and a cytoplasmic tail. The expression of Siglec-F is restricted to the cells of myelomonocytic lineage. Mouse Siglec-F is likely an ortholog of human Siglec-5. Unlike many human CD33-related Siglecs, which show similar binding to both alpha 2,3- and alpha 2,6-linked sialic acids, mouse Siglec-F preferentially recognize alpha 2,3-linked sialic acid.