Mouse Endoglin/CD105 Fluorescein-conjugated Antibody

Catalog # Availability Size / Price Qty
FAB1320F-100
FAB1320F-025
Detection of Endoglin/CD105 in MS‑1 Mouse Cell Line by Flow Cytometry.
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Product Details
Citations (5)
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Mouse Endoglin/CD105 Fluorescein-conjugated Antibody Summary

Species Reactivity
Mouse
Specificity
Detects mouse Endoglin/CD105 in direct ELISAs and Western blots. In Western blots, this antibody shows 100% cross-reactivity with recombinant human Endoglin/CD105.
Source
Monoclonal Rat IgG2A Clone # 209701
Purification
Protein A or G purified from hybridoma culture supernatant
Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse Endoglin/CD105
Glu21-Gly581 (predicted)
Accession # NP_031958
Formulation
Supplied in a saline solution containing BSA and Sodium Azide.
Label
Fluorescein (Excitation= 488 nm, Emission= 515-545 nm)

Applications

Recommended Concentration
Sample
Flow Cytometry
10 µL/106 cells
See below

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Flow Cytometry Detection of Endoglin/CD105 antibody in MS‑1 Mouse Cell Line antibody by Flow Cytometry. View Larger

Detection of Endoglin/CD105 in MS‑1 Mouse Cell Line by Flow Cytometry. MS-1 mouse pancreatic islet endothelial cell line was stained with Rat Anti-Mouse Endoglin/CD105 Fluorescein-conjugated Monoclonal Antibody (Catalog # FAB1320F, filled histogram) or isotype control antibody (Catalog # IC006F, open histogram). View our protocol for Staining Membrane-associated Proteins.

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Preparation and Storage

Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
  • 12 months from date of receipt, 2 to 8 °C as supplied.

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% 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 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 BMP-7 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 (sFlt-1), along with low Placental Growth Factor (PlGF), are pathogenic due to anti-angiogenic activity (15).

References
  1. Ge, A.Z. and E.C. Butcher (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.
Entrez Gene IDs
2022 (Human); 13805 (Mouse); 497010 (Rat)
Alternate Names
CD105 antigen; CD105; Endoglin; ENDOsler-Rendu-Weber syndrome 1; ENG; HHT1FLJ41744; ORW; ORW1

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Citations for Mouse Endoglin/CD105 Fluorescein-conjugated Antibody

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.

5 Citations: Showing 1 - 5
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  1. Efficacy of Photobiomodulation and Metformin on Diabetic Cell Line of Human Periodontal Ligament Stem Cells through Keap1/Nrf2/Ho-1 Pathway
    Authors: Latifa Mohamed Abdelgawad, Manar Mohy Abd El-hamed, Dina Sabry, Marwa Abdelgwad, Department of Medical Laser applications, National Institute of laser enhanced science, Cairo University, Egypt., Department of Medical Laser application, National Institute of laser enhanced science, Cairo University, Egypt et al.
    Reports of Biochemistry and Molecular Biology
  2. BMP-non-responsive Sca1+ CD73+ CD44+ mouse bone marrow derived osteoprogenitor cells respond to combination of VEGF and BMP-6 to display enhanced osteoblastic differentiation and ectopic bone formation.
    Authors: Madhu V, Li C, Dighe A, Balian G, Cui Q
    PLoS ONE, 2014-07-21;9(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  3. Adenosine A2A receptors play an active role in mouse bone marrow-derived mesenchymal stem cell development.
    Authors: Katebi M, Soleimani M, Cronstein BN
    J. Leukoc. Biol., 2008-12-12;85(3):438-44.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  4. PEDF from mouse mesenchymal stem cell secretome attracts fibroblasts.
    Authors: Sarojini H, Estrada R, Lu H, Dekova S, Lee MJ, Gray RD, Wang E
    J. Cell. Biochem., 2008-08-01;104(5):1793-802.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  5. Influence of photobiomodulation and vitamin D on osteoblastic differentiation of human periodontal ligament stem cells and bone-like tissue formation through enzymatic activity and gene expression
    Authors: Latifa Mohamed Abdelgawad, Asmaa Mohamed Abdelaziz, Dina Sabry, Marwa Abdelgwad
    Biomolecular Concepts

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