SPN
SPN (sialophorin), also known as leukosialin, CD43, LSN, GPL115 and LEU-22, is a highly sialylated cell-surface glycoprotein that functions in antigen-specific activation of T cells. It also protects cells from apoptotic signals, promoting cell survival. Browse Assay Genie's current range of SPN research reagents below, or read on for the biology behind the target.
SPN is a highly sialylated glycoprotein that functions in the antigen-specific activation of T cells. It is found on the surface of thymocytes, T lymphocytes, monocytes, granulocytes and some B lymphocytes. UniProt also annotates a role in protecting cells from apoptotic signals, which promotes cell survival. Together these activities place SPN at the interface between immune cell activation and cell fate.
The SPN gene encodes a protein with three regions: a mucin-like extracellular domain, a transmembrane region and a carboxy-terminal intracellular region. The extracellular domain contains a high proportion of serine and threonine residues, which allows extensive O-glycosylation, and it has one potential N-glycosylation site. The carboxy-terminal region carries potential phosphorylation sites that may mediate the transduction of activation signals. UniProt lists the protein at the membrane, including microvilli and the uropodium, and also in the nucleus, where it is found in PML bodies.
Different glycoforms of SPN have been described. In stimulated immune cells, proteolytic cleavage of the extracellular domain occurs in some cell types and releases a soluble extracellular fragment. Defects in expression of the SPN gene are associated with Wiskott-Aldrich syndrome.
The protein is known by several names. HGNC approves sialophorin as the full name and previously listed gpL115, leukosialin and CD43. Aliases include LSN, GPL115 and LEU-22, and the gene belongs to the HGNC group of CD molecules. The mouse ortholog is written Spn, which is relevant when moving between human and murine models.
SPN functions in antigen-specific activation of T cells, and its intracellular region has potential phosphorylation sites that may transduce activation signals.
SPN protects cells from apoptotic signals and promotes cell survival, making it relevant to studies of how immune cells resist death.
Its serine- and threonine-rich extracellular domain is extensively O-glycosylated, and distinct glycoforms have been described, so SPN suits studies of sialylation.
Defects in SPN expression are associated with Wiskott-Aldrich syndrome, linking the protein to this immunodeficiency disorder.
SPN is a highly sialylated glycoprotein that functions in antigen-specific activation of T cells. UniProt annotates it as protecting cells from apoptotic signals and promoting cell survival. Its intracellular region has potential phosphorylation sites that may mediate transduction of activation signals.
Yes. HGNC lists sialophorin as the approved name, with gpL115, leukosialin and CD43 as previous names. The aliases LSN, GPL115 and LEU-22 also refer to the same gene. The gene is classed among the CD molecules.
SPN is found on thymocytes, T lymphocytes, monocytes, granulocytes and some B lymphocytes. Defects in its expression are associated with Wiskott-Aldrich syndrome. The mouse ortholog is Spn; check the datasheet of any product for its validated reactivity.
Other CD molecules, T cell markers and immune-cell glycoproteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P16150; product specifications from Assay Genie datasheets.