Home / Endoglin/CD105 / Human Endoglin/CD105 Antibody

Human Endoglin/CD105 Antibody

Catalog #: MAB1097
4 Citations Datasheet
Catalog # Availability Size / Price Qty
MAB1097
MAB1097-SP
Product Details
Citations (4)
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Summary Preparation and Storage Reconstitution Calculator Background Product Datasheets Related Research Areas

Human Endoglin/CD105 Antibody Summary

Species Reactivity
Human
Specificity
Detects human Endoglin/CD105 in direct ELISAs and Western blots. In direct ELISAs and Western blots, this antibody shows 10-50% cross-reactivity with recombinant mouse Endoglin.
Source
Monoclonal Mouse IgG1 Clone # 166709
Purification
Protein A or G purified from hybridoma culture supernatant
Immunogen
Mouse myeloma cell line NS0-derived recombinant human Endoglin/CD105
Glu26-Gly256
Accession # Q5T9B9
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Applications

Recommended Concentration
Sample
Western Blot
1 µg/mL
Recombinant Human Endoglin/CD105 (Catalog # 1097-EN)
under non-reducing conditions only

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.

Preparation and Storage

Reconstitution
Reconstitute at 0.5 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store 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.
  • 6 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 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-IA/ALK-3 or BMPR-IB/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/ALK-5, 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 (sFlt-1), 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

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Citations for Human Endoglin/CD105 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.

4 Citations: Showing 1 - 4
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  1. 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: Cell Lysates, Whole Tissue
    Applications: IHC, Western Blot
  2. 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: Cell Lysates
    Applications: Western Blot
  3. Induction of an epithelial integrin alphavbeta6 in human cytomegalovirus-infected endothelial cells leads to activation of transforming growth factor-beta1 and increased collagen production.
    Authors: Tabata T, Kawakatsu H, Maidji E, Sakai T, Sakai K, Fang-Hoover J, Aiba M, Sheppard D, Pereira L
    Am. J. Pathol., 2008-03-18;172(4):1127-40.
    Species: Human
    Sample Types: Cell Lysates, Whole Cells
    Applications: Flow Cytometry, Western Blot
  4. Microglial transcription profiles in mouse and human are driven by APOE4 and sex
    Authors: Moser V, Workman M, Hurwitz S Et al.
    iScience

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