Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SIGLEC6 in samples. An antibody specific for SIGLEC6 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySIGLEC6 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SIGLEC6 is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of SIGLEC6 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:The deduced 442-amino acid CD33L protein contains a signal peptide, an N-terminal Ig-like V-domain, and 2 adjacent Ig C2-like domains, followed by a transmembrane region and a cytoplasmic tail. Based on its predicted structure, the authors stated that CD33L belongs to the Ig superfamily and is likely a novel member of the sialoadhesin subfamily. Compared to the original cDNA, this cDNA contains a 176-bp deletion in the coding sequence, resulting in a predicted 342-amino acid protein lacking the transmembrane and cytoplasmic regions. By RT-PCR of placenta RNA, the authors detected both transcripts, although the transcript encoding the membrane-bound isoform, CD33L1, was considerably more abundant.CD33L expression only in the placenta; transcripts of 4 distinct sizes were found, including 1 that was differentially polyadenylated.
