Recombinant Human Endoglin/CD105 Protein Summary
Product Specifications
Glu26-Gly586
Analysis
Product Datasheets
1097-EN (with carrier)
1097-EN/CF (carrier free)
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
1097-EN
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 250 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
1097-EN/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 250 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: Endoglin/CD105
Endoglin (CD105) is a 90 kDa type I transmembrane glycoprotein of the zona pellucida (ZP) family of proteins (1‑3). Endoglin and betaglycan/T beta RIII 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 beta RII (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 beta RI/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).
- Gougos, A. and Letarte, M. (1990) J. Biol. Chem. 265:8361.
- ten Dijke, P. et al. (2008) Angiogenesis 11:79.
- Bernabeu, C. et al. (2007) J. Cell. Biochem. 102:1375.
- Mancini, M.L. et al. (2007) Dev. Biol. 308:520.
- Moody, J.L. et al. (2007) Stem Cells 25:2809.
- Velasco, S. et al. (2008) J. Cell Sci. 121:913.
- Perez-Gomez, E. et al. (2005) Oncogene 24:4450.
- Cheifetz, S, et al. (1992) J. Biol. Chem. 267:19027.
- Barbara, N.P. et al. (1999) J. Biol. Chem. 274:584.
- Scharpfenecker, M. et al. (2007) J. Cell Sci. 120:964.
- Scherner, O. et al. (2007) J. Biol. Chem. 282:13934.
- Pece-Barbara, N. et al. (2005) J. Biol. Chem. 280:27800.
- Arthur, H.M. et al. (2000) Dev. Biol. 217:42.
- Lebrin, F. and C.L. Mummery (2008) Trends Cardiovasc. Med. 18:25.
- Venkatesha, S. et al. (2006) Nat. Med. 12:642.
Citations for Recombinant Human Endoglin/CD105 Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 10
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Regulation and Release of Vasoactive Endoglin by Brain Endothelium in Response to Hypoxia/Reoxygenation in Stroke
Authors: A Haarmann, L Zimmermann, M Bieber, C Silwedel, G Stoll, MK Schuhmann
International Journal of Molecular Sciences, 2022-06-25;23(13):.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Soluble Endoglin Stimulates Inflammatory and Angiogenic Responses in Microglia That Are Associated with Endothelial Dysfunction
Authors: ES Park, S Kim, DC Yao, JPJ Savarraj, HA Choi, PR Chen, E Kim
International Journal of Molecular Sciences, 2022-01-22;23(3):.
Species: Mouse
Sample Types: In Vivo
Applications: Bioassay -
Pregnancy-Induced High Plasma Levels of Soluble Endoglin in Mice Lead to Preeclampsia Symptoms and Placental Abnormalities
Authors: L Pérez-Roqu, E Núñez-Góme, A Rodríguez-, C Bernabéu, JM López-Novo, M Pericacho
International Journal of Molecular Sciences, 2020-12-26;22(1):.
Species: Human
Sample Types: Whole Cells
Applications: Cell Culture -
Potential Role of Circulating Endoglin in Hypertension via the Upregulated Expression of BMP4
Authors: E Gallardo-V, L Gamella-Po, L Perez-Roqu, JL Bartha, I Garcia-Pal, JI Casal, JM López-Novo, M Pericacho, C Bernabeu
Cells, 2020-04-16;9(4):.
Species: Human
Sample Types: Whole Cells
Applications: Cell Culture -
Fibrinogen induces neural stem cell differentiation into astrocytes in the subventricular zone via BMP signaling
Authors: L Pous, SS Deshpande, S Nath, S Mezey, SC Malik, S Schildge, C Bohrer, K Topp, D Pfeifer, F Fernández-, S Doostkam, DK Galanakis, V Taylor, K Akassoglou, C Schachtrup
Nat Commun, 2020-01-31;11(1):630.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Endoglin Protein Interactome Profiling Identifies TRIM21 and Galectin-3 as New Binding Partners
Authors: E Gallardo-V, L Ruiz-Llore, J Casado-Vel, MJ Ruiz-Rodrí, N López-Andr, AK Pattnaik, M Quintanill, C Bernabeu
Cells, 2019-09-13;8(9):.
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay, Bio-Layer Interferometry (BLI) -
Microglial Phenotyping in Neurodegenerative Disease Brains: Identification of Reactive Microglia with an Antibody to Variant of CD105/Endoglin
Authors: DG Walker, LF Lue, TG Beach, I Tooyama
Cells, 2019-07-23;8(7):.
Species: Human
Sample Types: Protein
Applications: Bioassay -
Circulating soluble endoglin modifies the inflammatory response in mice
Authors: L Ruiz-Remol, C Ollauri-Ib, L Pérez-Roqu, E Núñez-Góme, F Pérez-Barr, JM López-Novo, M Pericacho, A Rodríguez-
PLoS ONE, 2017-11-16;12(11):e0188204.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Bone morphogenetic protein-9 suppresses growth of myeloma cells by signaling through ALK2 but is inhibited by endoglin.
Authors: Olsen O, Wader K, Misund K, Vatsveen T, Ro T, Mylin A, Turesson I, Stordal B, Moen S, Standal T, Waage A, Sundan A, Holien T
Blood Cancer J, 2014-03-21;4(0):e196.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Endothelial endoglin is involved in inflammation: role in leukocyte adhesion and transmigration.
Authors: Rossi E, Sanz-Rodriguez F, Eleno N, Duwell A, Blanco F, Langa C, Botella L, Cabanas C, Lopez-Novoa J, Bernabeu C
Blood, 2012-10-16;121(2):403-15.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Matrix metalloproteinase-14 (MT1-MMP)-mediated endoglin shedding inhibits tumor angiogenesis.
Authors: Hawinkels LJ, Kuiper P, Wiercinska E
Cancer Res., 2010-04-27;70(10):4141-50.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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