Human Endoglin/CD105 (His Tag) recombinant protein

Human Endoglin/CD105 (His Tag) recombinant protein

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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-? superfamily ligands, endoglin binds TGF-?1 and TGF-?3 with high affinity not by itself but by associating with TGF-? type I I receptor (T?RII) 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 (Osler-Rendu-Weber syndrome 1), isoform CRA_a

Q96CG0

ENG; hCG_18549

Human Cells

A DNA sequence encoding the extracellular domain of human CD105 (NP_001108225.1) (Met 1-Gly 586) was expressed, with C-terminal fused polyhistidine tag.

Human

The recombinant human CD105 consists of 572 amino acids after removal of the signal peptide and predicts a molecular mass of 62.3 kDa. As a result of glycosylation, rh CD105 migrates as an approximately 80-90 kDa protein in SDS-PAGE under reducing conditions.

> 95 % as determined by SDS-PAGE