Basal Cell Adhesion Molecule (BCAM) which is a product of alternate splicing of the Lutheran blood group molecule is a part of the immunoglobulin superfamily. BCAM contains five extracellular immunoglobulin domains, a single transmembrane domain, and a short C-terminal cytoplasmic tail. BCAM protein is upregulated following malignant transformation of some cell types in vivo and in vitro. Furthermore, BCAM interacts with integrin in sickle red cells, and participates in vasoocclusive episodes.
BCAM produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 755 amino acids (32-547a.a.) and having a molecular mass of 83.2kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). BCAM is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
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