Recombinant Human VE-Cadherin Fc Chimera His-tag Protein, CF

Catalog # Availability Size / Price Qty
938-VC-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human VE-Cadherin Fc Chimera His-tag Protein, CF Summary

Product Specifications

Purity
>95%, 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 the ability of the immobilized protein to support the adhesion of BCE C/D‑1b bovine corneal endothelial cells. The ED50 for this effect is 40-160 ng/mL.
Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human VE-Cadherin protein
Human VE-Cadherin
(Asp48-Gln593)
Accession # P33151
IEGRMD Human IgG1
(Pro100-Lys330)
6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Analysis
Asp48
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
89 kDa (monomer)
SDS-PAGE
116 kDa, reducing conditions

Product Datasheets

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938-VC

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.

938-VC

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 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.
  • 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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Reconstitution Calculator

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Background: VE-Cadherin

VE-Cadherin, also known as Cadherin-5 and CD144, is a member of the atypical/type II subgroup of Cadherin homophilic adhesion proteins (1). Mature human VE-Cadherin is a 125-135 kDa transmembrane glycoprotein that consistis of a 552 amino acid (aa) extracellular domain (ECD) with five Ca++-binding Cadherin domains, a 21 aa transmembrane segment, and a 164 aa cytoplasmic domain (2, 3). Within the ECD, human VE-Cadherin shares approximately 75% aa sequence identity with mouse and rat VE-Cadherin. A 90 kDa portion of the VE-Cadherin ECD can be shed in a metalloproteinase-dependent mechanism and may function as a VE-Cadherin antagonist (4, 5). VE-Cadherin is expressed on the surface of vascular endothelial cells (EC) from early in embryogenesis through adulthood as well as in the placenta, on hematopoietic cell progenitors, and on a subpopulation of hematopoietic stem cells (6-8). It is a major protein component of adherens junctions between cells of the endothelium (9). VE-Cadherin supports the extension and stabilization of existing vascular sprouts (10). VE-Cadherin also regulates or is regulated by VEGF R2, type I and type II TGF-beta receptors, and other endothelial junction proteins such as JAM-C, Claudin-5, and N-Cadherin (11-15). Elevated levels of soluble VE-Cadherin are found in the serum of myocardial infarction, angina pectoris, rheumatoid arthritis, and colorectal cancer patients (16-18).

References
  1. Giannotta, M. et al. (2013) Dev. Cell 26:441.
  2. Breviario, F. et al. (1995) Arterioscler. Throm. Vasc. Biol. 15:1229.
  3. Geyer, H. et al. (1999) Glycobiology 9:915.
  4. Herren, B. et al. (1998) Mol. Biol. Cell 9:1589.
  5. Li, H. et al. (2010) Cancer Gene Ther. 17:700.
  6. Breier, G. et al. (1996) Blood 87:630.
  7. Ema, M. et al. (2006) Blood 108:4018.
  8. Oberlin, E. et al. (2010) Blood 116:4444.
  9. Lampugnani, M.G. et al. (1992) J. Cell Biol. 118:1511.
  10. Perryn, E.D. et al. (2008) Dev. Biol. 313:545.
  11. Gavard, J. and J.S. Gutkind (2006) Nat. Cell Biol. 8:1223.
  12. Orlova, V.V. et al. (2006) J. Exp. Med. 203:2703.
  13. Taddei, A. et al. (2008) Nat. Cell Biol. 10:923.
  14. Luo, Y. and G.L. Radice (2005) J. Cell Biol. 169:29.
  15. Rudini, N. et al. (2008) EMBO J. 27:993.
  16. Soeki, T. et al. (2004) Circ. J. 68:1.
  17. Sulkowska, M. et al. (2006) Tumori 92:67.
  18. Sidibe, A. et al. (2012) Arthritis Rheum. 64:77.
Long Name
Vascular Endothelium Cadherin
Entrez Gene IDs
1003 (Human); 12562 (Mouse)
Alternate Names
7B4 antigen; 7B4; cadherin 5, type 2 (vascular endothelium); cadherin 5, type 2, VE-cadherin (vascular epithelium); Cadherin-5; CD144 antigen; CD144; CDH5; endothelial-specific cadherin; FLJ17376; Vascular endothelial cadherin; VECadherin; VE-Cadherin

Citations for Recombinant Human VE-Cadherin Fc Chimera His-tag 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.

4 Citations: Showing 1 - 4
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  1. Neuropilin 1 and its inhibitory ligand mini-tryptophanyl-tRNA synthetase inversely regulate VE-cadherin turnover and vascular permeability
    Authors: N Gioelli, LJ Neilson, N Wei, G Villari, W Chen, B Kuhle, M Ehling, F Maione, S Willox, S Brundu, D Avanzato, G Koulouras, M Mazzone, E Giraudo, XL Yang, D Valdembri, S Zanivan, G Serini
    Nature Communications, 2022-07-20;13(1):4188.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  2. Mutant B-Raf(V600E) Promotes Melanoma Paracellular Transmigration by Inducing Thrombin-mediated Endothelial Junction Breakdown.
    Authors: Zhang P, Feng S, Liu G, Wang H, Zhu H, Ren Q, Bai H, Fu C, Dong C
    J Biol Chem, 2015-10-26;291(5):2087-106.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Cadherin 6 has a functional role in platelet aggregation and thrombus formation.
    Authors: Dunne E, Spring CM, Reheman A, Jin W, Berndt MC, Newman DK, Newman PJ, Ni H, Kenny D
    Arterioscler. Thromb. Vasc. Biol., 2012-04-26;32(7):1724-31.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Lentiviral rescue of vascular endothelial growth factor receptor-2 expression in flk1-/- embryonic stem cells shows early priming of endothelial precursors.
    Authors: Li X, Edholm D, Lanner F, Breier G, Farnebo F, Dimberg A, Claesson-Welsh L
    Stem Cells, 2007-08-16;25(12):2987-95.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay

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