CD103 is a type I transmembrane glycoprotein known as αE integrin or Integrin αIEL chain. It belongs to the integrin family and is primarily found on intestinal intraepithelial lymphocytes (IEL). CD103 is also expressed on a subpopulation of lamina propria T cells, epithelial dendritic cells, lamina propria-derived dendritic cells, and a small subset of peripheral lymphocytes. T regulatory cells express high level of CD103. The CD103 expression on lymphocytes can be induced upon activation and TGF-β stimulation. In association with integrin β7, CD103 is expressed as αE/β7 heterodimer. Mature CD103 protein can be cleaved into 2 chains, a 150 kD (C-terminal) chain and a 25 kD (N-terminal) chain, which remain linked by disulfide bonds. CD103 binds to E-cadherin and mediates homing of lymphocytes to the intestinal epithelium.
CD105 is a 90 kD homodimeric type I integral membrane glycoprotein, also known as endoglin. It is expressed on endothelial cells (especially on angiogenic endothelial cells) and upregulated by hypoxia, activated monocytes, macrophages, bone marrow stromal cells, and some cytotrophoblasts. CD105 is a receptor for TGF-β1, TGF-β3 and modulates TGF-β signaling by interacting with TGF-β receptors I and/or II. CD105 also binds other growth factors such as actvin A, BMP-2, and BMP-7. CD105 has been show to be a useful marker for identifying proliferating endothelium involved in tumor angiogenesis and can be used for tumor imaging and prognosis, and has therapeutic potential for some solid tumors and other angiogenic diseases.
CD106 is a 110 kD glycosylphosphatidylinositol (GPI)-linked transmembrane protein, also known as VCAM-1 and INCAM-110. It is constitutively expressed on bone marrow stromal cells, myeloid progenitors, splenic dendritic cells, activated endothelial cells, as well as some lymphocytes. CD106 expression can be upregulated on endothelial cells by inflammatory cytokines. CD106 is involved in adhesion and acts as a counter-receptor for VLA-4 (α4/β1 integrin) and LPAM-1 (α4/β7 integrin).
The 1D4B antibody recognizes CD107a which is also known as, Lysosome-Associated Membrane Protein 1 (LAMP-1). CD107a is one of the two major glycoproteins in lysosome membranes that provide useful markers to distinguish lysosomes from other organelles. CD107a may play a role in the lysosomal degradation of certain molecules. Mouse CD107a is a type I transmembrane glycoprotein. It consists of a 40-kDa core protein which is heavily glycosylated to form heterogeneous mature glycoprotein of 110-140 kDa. It is principally expressed in epithelial cells and macrophages in a variety of organs. Following activation, CD107a is relocated to the surface of some lymphocytes, macrophages, epithelial cells, endothelial cells, platelets, and tumor cells. Cell-surface CD107a may participate in intercellular adhesion and adhesion to the extracellular matrix. Cell surface CD107a expression can serve as a useful marker for cytotoxic NK and CD8+ T cells, as well as, some malignant tumor cells.
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