Endoglin/CD105 Proteins, Antibodies, cDNA Clones, ELISA Kits Research Reagents

All Endoglin/CD105 reagents are produced in house and quality controlled, including 33 Endoglin/CD105 Antibody, 4 Endoglin/CD105 ELISA, 39 Endoglin/CD105 Gene, 1 Endoglin/CD105 IP Kit, 3 Endoglin/CD105 Lysate, 3 Endoglin/CD105 Protein, 3 Endoglin/CD105 qPCR. All Endoglin/CD105 reagents are ready to use.

All Endoglin/CD105 Reagents

Endoglin/CD105 Protein (3)

    Endoglin/CD105 Antibody (33)

      Endoglin/CD105 ELISA Kit & Match Antibody ELISA Pair Set (4)

      Endoglin/CD105 cDNA Clone (39)


      Endoglin/CD105 Lysate (3)

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        Endoglin/CD105 Background

        Endoglin, also known as CD15, is a type I homodimeric transmembrane glycoprotein with a large, disulfide-linked, extracellular region and a short, constitutively phosphorylated cytoplasmic tail. Endoglin contains an RGD tripeptide which is a key recognition structure in cellular adhesion,,suggesting a critical role for endoglin in the binding of endothelial cells to integrins and/or other RGD receptors. Endoglin is highly expressed on vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta. It is also found on activated monocytes, mesenchymal stem cells and leukemic cells of lymphoid and myeloid lineages. As an accessory receptor for the TGF-β superfamily ligands, endoglin binds TGF-β1 and TGF-β3 with high affinity not by itself but by associating with TGF-β type II receptor (TβRII) and activates the downstream signal pathways. In addition, in human umbilical vein endothelial cells, ALK-1 is also a receptor kinase for endoglin threonine phosphorylation, and mutations in either of the two genes result in the autosomal-dominant vascular dysplasia, hereditary hemorrhagic telangiectasia (HHT). Endoglin has been regarded as a powerful biomarker of neovascularization, and is associated with several solid tumor types.

        Endoglin/CD105 References

        • Bellon T., et al.,(1993), Identification and expression of two forms of the human transforming growth factor-beta-binding protein endoglin with distinct cytoplasmic regions. Eur. J. Immunol. 23:2340-2345.
        • Humphray S.J., et al., (2004), DNA sequence and analysis of human chromosome 9.Nature 429:369-374.
        • Gougos A., et al.,(1990), Primary structure of endoglin, an RGD-containing glycoprotein of human endothelial cells.J. Biol. Chem. 265:8361-8364.

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