Human sialic acid-binding Ig-like lectin 14 (Siglec 14) is a Type I transmembrane protein and a member of the Siglec family and immunoglobulin superfamily. The recombinant Siglec 14 dimer protein (CSP-25210-01) is a cis-homodimer (cis-dimer) and contains a Siglec 14 extracellular domain (UniProt# Q08ET2, amino acids Glu17-Leu358) fused with a proprietary cis-dimer motif followed by a His tag at the C-terminus. This dimeric protein is expressed in HEK293T cells. The recombinant human Siglec 14 dimer protein can potently bind Siglec 14-specific antibodies. This Siglec 14 dimer can be used as an antigen for in vitro assays and antibody screening, and as an immunogen for immunization to generate antibodies targeting more conformational epitopes.
Protein Name: Siglec 14
UniProt #: Q08ET2
Predicted Molecular Weight: 92 kDa
SDS PAGE Molecular Weight: The migration range of the heterodimer protein with glycosylation under non-reducing condition is between 120 and 190 kDa on SDS PAGE.
Protein Construct: Siglec 14 dimer protein contains a Siglec 14 extracellular domainfused with a proprietary cis-dimer motif followed by a His tag at the C-terminus.
Background
Human sialic acid-binding Ig-like lectin 14 (Siglec 14, Siglec-14) is a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. Siglec 14 is part of the immunoglobulin superfamily, and a multifunctional immune regulator in the innate immune system. Siglec 14 is a Type I transmembrane protein and can form homodimers on the cell surface. It contains an extracellular domain with three immunoglobulin-like (Ig-like) domains followed by a transmembrane domain and cytoplasmic signaling domain. The Siglec 14 cytoplasmic signaling domain lacks the typical immunoreceptor tyrosine-based inhibitory motif (ITIM) of other Siglecs, instead containing a positively charged “essential arginine” critical for interaction with adaptor molecules DAP10 and DAP12. When bound to DAP10 or DAP12, Siglec 14 activates cellular pathways while Siglec 5 inhibits them. Siglec 14 and Siglec 5 colocalize and are “paired receptors” meaning they show high mutual sequence similarity and have antagonizing signaling activities. Siglec 14 is expressed on myeloid cells and binds sialylated glycans on cell surfaces or secreted proteins, modulating cell-cell interactions and immune responses. Siglec 14 recognizes bacterial pathogens and elicits pro-inflammatory responses.
MW: Molecular Weight marker reduced condition
NR: Siglec 14 dimer under non-reduced condition
Immobilized human Siglec 14 protein dimer