Recombinant Human Endoglin/CD105 Fc Chimera Protein, CF

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6578-EN-025
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human Endoglin/CD105 Fc Chimera Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to inhibit BMP-10-induced alkaline phosphatase production by MC3T3‑E1 mouse preosteoblast cells. The ED50 for this effect is 0.3-1.2 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human Endoglin/CD105 protein
Human Endoglin
(Met1-Gly586)
Accession # P17813
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Analysis
Glu26
Predicted Molecular Mass
87.3 kDa (monomer)
SDS-PAGE
100-115 kDa, reducing conditions

Product Datasheets

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6578-EN

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

6578-EN

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 250 μg/mL in 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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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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 with within 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 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).

References
  1. Gougos, A. and Letarte, M. (1990) J. Biol. Chem. 265:8361.
  2. ten Dijke, P. et al. (2008) Angiogenesis 11:79.
  3. Bernabeu, C. et al. (2007) J. Cell. Biochem. 102:1375.
  4. Mancini, M.L. et al. (2007) Dev. Biol. 308:520.
  5. Moody, J.L. et al. (2007) Stem Cells 25:2809.
  6. Velasco, S. et al. (2008) J. Cell Sci. 121:913.
  7. Perez-Gomez, E. et al. (2005) Oncogene 24:4450.
  8. Cheifetz, S, et al. (1992) J. Biol. Chem. 267:19027.
  9. Barbara, N.P. et al. (1999) J. Biol. Chem. 274:584.
  10. Scharpfenecker, M. et al. (2007) J. Cell Sci. 120:964.
  11. Scherner, O. et al. (2007) J. Biol. Chem. 282:13934.
  12. Pece-Barbara, N. et al. (2005) J. Biol. Chem. 280:27800.
  13. Arthur, H.M. et al. (2000) Dev. Biol. 217:42.
  14. Lebrin, F. and C.L. Mummery (2008) Trends Cardiovasc. Med. 18:25.    
  15. Venkatesha, S. et al. (2006) Nat. Med. 12:642.
Entrez Gene IDs
2022 (Human); 13805 (Mouse); 497010 (Rat)
Alternate Names
CD105 antigen; CD105; Endoglin; ENDOsler-Rendu-Weber syndrome 1; ENG; HHT1FLJ41744; ORW; ORW1

Citations for Recombinant Human Endoglin/CD105 Fc Chimera Protein, CF

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.

2 Citations: Showing 1 - 2
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  1. TGF-? contamination of purified recombinant GDF15
    Authors: OE Olsen, A Skjærvik, BF Størdal, A Sundan, T Holien
    PLoS ONE, 2017;12(11):e0187349.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Soluble Endoglin Specifically Binds Bone Morphogenetic Proteins 9 and 10 via Its Orphan Domain, Inhibits Blood Vessel Formation, and Suppresses Tumor Growth.
    Authors: Castonguay R, Werner ED, Matthews RG, Presman E, Mulivor AW, Solban N, Sako D, Pearsall RS, Underwood KW, Seehra J, Kumar R, Grinberg AV
    J. Biol. Chem., 2011;286(34):30034-46.
    Species: Chicken
    Sample Types: Whole Cells
    Applications: Bioassay

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