Recombinant Mouse Endoglin/CD105 Fc Chimera Protein, CF

Catalog # 1320-EN | R&D Systems, Inc. a Bio-Techne Brand
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1320-EN-025
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Key Product Details

Accession #

Q8K100

Source

NS0

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

Mouse myeloma cell line, NS0-derived mouse Endoglin/CD105 protein
Mouse Endoglin
(Glu27-Gly581)
Accession # Q8K100		 IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Glu27

Predicted Molecular Mass

86 kDa (monomer)

SDS-PAGE

100-110 kDa, reducing conditions

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 0.15-0.75 μg/mL.

Formulation, Preparation and Storage

1320-EN
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 100 μg/mL in sterile PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.

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 betaRIII are type III receptors for TGF beta superfamily ligands, sharing 71% amino acid (aa) identity 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). Mouse Endoglin cDNA encodes 653 aa including a 26 aa signal sequence, a 555 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). A mouse isoform with a 35 aa cytoplasmic domain (S-endoglin) can oppose effects of long (L) Endoglin (6, 7). The mouse Endoglin ECD shares 69%, 84%, 62%, 63% and 66% aa identity with human, rat, bovine, porcine and canine Endoglin, respectively. 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).

References

  1. Ge, A.Z. and Butcher, E.C. (1994) Gene 138:201.
  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.

Alternate Names

CD105, ENG

Entrez Gene IDs

2022 (Human); 13805 (Mouse); 497010 (Rat)

Gene Symbol

ENG

UniProt

Q8K100

Product Documents for Recombinant Mouse Endoglin/CD105 Fc Chimera Protein, CF

Certificate of Analysis

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Product Specific Notices for Recombinant Mouse Endoglin/CD105 Fc Chimera Protein, CF

For research use only

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