The B-A38 monoclonal antibody specifically recognizes an extracellular epitope on human CD138 that is also known as Syndecan-1 (SDC-1). CD138 is a transmembrane type I and surface heparan sulfate proteoglycan that is expressed as an ~65-70 kDa core protein dimer with variable glycosylation. CD138 is encoded by SDC1 (syndecan 1) which belongs to the syndecan proteoglycan family. CD138 is expressed on pre-B cells, immature B cells, and plasma cells, but not on mature circulating B-lymphocytes, as well as by embryonic mesenchymal cells and certain epithelial and endothelial cells. It is strongly expressed on multiple-myeloma-derived cell lines and malignant plasma cell populations. CD138 is involved in many cellular functions including cell-cell and cell matrix adhesion. It binds to multiple extracellular matrix (ECM) proteins and soluble bioactive factors through its heparan sulfate side chains. ECM protein ligands for CD138 include fibronectin, certain collagens, tenascin, thrombospondin, and antithrombin III. Certain cytokines and growth factors are bound by CD138 and accumulated on CD138-positive cells which contributes to the sensitive recognition and response to these factors by neighboring cells. These may include fibroblast, hepatocyte, and epidermal growth factors and April. A soluble shed form of CD138 has also been described which can affect the stability and function of CD138.
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