Siglec-8 / Unconjugated / 7C9
Product Details
| Description | SIGLEC8 is a sialic acid binding lectin similar to CD33. In its cytoplasmic comain it contains an immunoreceptor tyrosine-based inhibitory motif (ITIM), and a motive similar to a binding site for SLAM-associated protein. SIGLEC8 is expressed e.g. in lymph nodes and spleen. It is an eosinophil marker, although it can be found also on the surface of mast cells. Crosslinking of SIGLEC8 leads to apoptosis. Soluble form of SIGLEC8 can be foud in human serum, especially in case of eosinophil-associated diseases. | |
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| Conjugate | Unconjugated | |
| Clone | 7C9 | |
| Target Species | Human | |
| Applications | ELISA, FC, IP | |
| Supplier | EXBIO | |
| Catalog # | Sign in to view product details, citations, and spectra | |
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About Siglec-8
Sialic acid-binding immunoglobulin (Ig)-like lectins, or SIGLECs (e.g., CD33 (MIM 159590)), are a family of type 1 transmembrane proteins each having a unique expression pattern, mostly in hemopoietic cells. SIGLEC8 is a member of the CD33-like subgroup of SIGLECs, which are localized to 19q13.3-q13.4 and have 2 conserved cytoplasmic tyrosine-based motifs: an immunoreceptor tyrosine-based inhibitory motif, or ITIM (see MIM 604964), and a motif homologous to one identified in signaling lymphocyte activation molecule (SLAM; MIM 603492) that mediates an association with SLAM-associated protein (SAP; MIM 300490) (summarized by Foussias et al., 2000 [PubMed 11095983]).[supplied by OMIM, May 2010]
Sialic acid-binding immunoglobulin (Ig)-like lectins, or SIGLECs (e.g., CD33 (MIM 159590)), are a family of type 1 transmembrane proteins each having a unique expression pattern, mostly in hemopoietic cells. SIGLEC8 is a member of the CD33-like subgroup of SIGLECs, which are localized to 19q13.3-q13.4 and have 2 conserved cytoplasmic tyrosine-based motifs: an immunoreceptor tyrosine-based inhibitory motif, or ITIM (see MIM 604964), and a motif homologous to one identified in signaling lymphocyte activation molecule (SLAM; MIM 603492) that mediates an association with SLAM-associated protein (SAP; MIM 300490) (summarized by Foussias et al., 2000 [PubMed 11095983]).[supplied by OMIM, May 2010]
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