Key Product Details
Product Summary for Human Endoglin/CD105 APC‑conjugated Antibody
Accession # Q5T9B9
Scientific Data Images for Human Endoglin/CD105 APC‑conjugated Antibody
Detection of Endoglin/CD105 in U937 Human Cell Line by Flow Cytometry.U937 human histiocytic lymphoma cell line was stained with Mouse Anti-Human Endoglin/CD105 APC-conjugated Mono-clonal Antibody (Catalog # FAB10971A, filled histogram) or isotype control antibody (Catalog # IC002A, open histogram). View our protocol for Staining Membrane-associated Proteins.
Applications for Human Endoglin/CD105 APC‑conjugated Antibody
Sample: U937 human histiocytic lymphoma cell line
Read 8 publications using FAB10971A in the following applications:
Formulation, Preparation and Storage
Stability & Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Endoglin (CD105) is a 90 kDa type I transmembrane glycoprotein of the zona pellucida (ZP) family of proteins (1‑3). Endoglin and betaglycan/T betaRIII are type III receptors for TGF beta superfamily ligands, sharing 71% aa identity in the transmembrane (TM) and cytoplasmic domains. Endoglin is highly expressed on proliferating vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta, with lower amounts on hematopoietic, mesenchymal and neural crest stem cells, activated monocytes, and lymphoid and myeloid leukemic cells (2‑5). Human Endoglin cDNA encodes 658 amino acids (aa) including a 25 aa signal sequence, a 561 aa extracellular domain (ECD) with an orphan domain and a two-part ZP domain, a TM domain and a 47 aa cytoplasmic domain (1‑3). An isoform with a 14 aa cytoplasmic domain (S-endoglin) can oppose effects of long (L) Endoglin (6, 7). The human Endoglin ECD shares 65-72% aa identity with mouse, rat, bovine, porcine and canine Endoglin. Endoglin homodimers interact with TGF-beta 1 and TGF-beta 3 (but not TGF-beta 2), but only after binding T betaRII (8). Similarly, they interact with activin-A and BMP-7 via activin type IIA or B receptors, and with BMP-2 via BMPR-1A/ALK-3 or BMPR-1B/ALK-6 (9). BMP-9, however, is reported to bind Endoglin directly (10). Endoglin modifies ligand-induced signaling in multiple ways. For example, expression of Endoglin can inhibit TGF-beta 1 signals but enhance BMP7 signals in the same myoblast cell line (11). In endothelial cells, Endoglin inhibits T betaRI/ALK5, but enhances ALK1-mediated activation (12). Deletion of mouse Endoglin causes lethal vascular and cardiovascular defects, and human Endoglin haploinsufficiency can a cause the vascular disorder, hereditary hemorrhagic telangiectasia type I (13, 14). These abnormalities confirm the essential function of Endoglin in differentiation of smooth muscle, angiogenesis, and neovascularization (2‑4, 12‑14). In preeclampsia of pregnancy, high levels of proteolytically generated soluble Endoglin and VEGF R1 (sFLT1), along with low placental growth factor (PlGF), are pathogenic due to antiangiogenic activity (15).
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Product Specific Notices for Human Endoglin/CD105 APC‑conjugated Antibody
For research use only