|Recombinant Mouse CD105 protein (Catalog#50407-M08H)|
|0.2 μm filtered solution in PBS|
|Produced in rabbits immunized with purified, recombinant Mouse ENG / CD105 extracellular domain (rM Endoglin; Catalog#50407-M08H; NP_031958.2; Met 1-Gly 580). ENG / CD105 specific IgG was purified by Mouse ENG / CD105 affinity chromatography.|
Anti-Histone H3 rabbit monoclonal antibody at 1:200 dilution
Lane A: NIH3T3 Whole Cell Lysate
Lane B: Hela Whole Cell Lysate
Lysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG (H+L)/HRP at 1/10000 dilution.
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size:15 kDa
Observed band size:17 kDa
Endoglin, also known as CD105, 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 I I 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.