Sialic Acid Binding Ig Like Lectin 14 (SIGLEC14)

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Sialic Acid Binding Ig Like Lectin 14 (SIGLEC14)
Human Siglec-14 has almost complete sequence identity with human Siglec-5 at the first two Ig-like domains, shows a glycan binding preference similar to that of human Siglec-5, and associates with the activating adapter protein DAP12. Thus, Siglec-14 and Siglec-5 appear to be the first glycan binding paired receptors. Near-complete sequence identity of the amino-terminal part of human Siglec-14 and Siglec-5 indicates partial gene conversion between SIGLEC14 and SIGLEC5. Remarkably, SIGLEC14 and SIGLEC5 in other primates also show evidence of gene conversions within each lineage. Evidently, balancing the interactions between Siglec-14, Siglec-5 and their common ligand(s) had selective advantage during the course of evolution. The "essential arginine" critical for sialic acid recognition in both Siglec-14 and Siglec-5 is present in humans but mutated in almost all great ape alleles.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPS344Hu01 Recombinant Sialic Acid Binding Ig Like Lectin 14 (SIGLEC14) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAS344Hu01 Polyclonal Antibody to Sialic Acid Binding Ig Like Lectin 14 (SIGLEC14) WB; ICC/IF
LAS344Hu71 Biotin-Linked Polyclonal Antibody to Sialic Acid Binding Ig Like Lectin 14 (SIGLEC14) WB; IHC; ICC.
Assay Kits SES344Hu ELISA Kit for Sialic Acid Binding Ig Like Lectin 14 (SIGLEC14) Enzyme-linked immunosorbent assay for Antigen Detection.
  1. "Discovery of Siglec-14, a novel sialic acid receptor undergoing concerted evolution with Siglec-5 in primates."FASEB J. 20:1964-1973(2006) [PubMed] [Europe PMC] [Abstract]
  2. "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]