Recombinant Mouse VE-Cadherin Fc Chimera Protein, CF

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Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse VE-Cadherin Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit proliferation of LL/2 mouse Lewis lung carcinoma cells. Immobilized rmVE-Cadherin/Fc Chimera inhibits LL/2 cell growth by 35-50%. The ED50 for this effect is 1.5-6.0 µg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse VE-Cadherin protein
Mouse VE-Cadherin
Asp46 - Gln592
Accession # 2208309A
IEGRMD Human IgG1
(Pro100 - Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Asp46
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Cdh5
Purity
>80%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
88.7 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
100-120 kDa, reducing conditions

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris-Citrate.
Purity
>80%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse VE-Cadherin Fc Chimera Protein, CF

  • 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

Background

The cadherin (Ca++-dependent adherence) superfamily is a large group of membrane-associated glycoproteins that engage in homotypic, calcium-dependent, cell-cell adhesion events. The superfamily can be divided into at least five major subfamilies based on molecule gene structure, and/or extracellular (EC) and intracellular domains (1, 2, 3, 4). Subfamilies include classical/type I, atypical/type II, and desmosomal-related cadherins (1, 2, 3). VE-Cadherin (vascular endothelial cadherin; also cadherin-5 and CD144) is a 125 kDa atypical/type II subfamily cadherin. Its subfamily classification is based principally on its genomic structure, as its physical structure is notably divergent from other type II subfamily members (2, 3). Mouse VE-Cadherin is synthesized as a 784 amino acid (aa) type I transmembrane (TM) preproprotein that contains a 24 aa signal peptide, a 21 aa prosequence, a 554 aa extracellular region (ECR), a 21 aa TM segment, and a 164 aa cytoplasmic domain (5, 6). The ECR contains five Ca++-binding cadherin domains that are approximately 105 aa in length. Cadherin domains are comprised of two beta -sheets that are oriented like bread in a sandwich. Although complex, the N-terminal cadherin domain mediates trans interactions, while the internal domains contribute to cis multimerizations (7). Mouse VE-Cadherin ECR is 92%, 77%, and 73% aa identical to rat, human and porcine VE-Cadherin ECR, respectively. VE-Cadherin is involved in the maintenance of endothelial permeability. In this regard, VE-Cadherin does not initiate new blood vessel formation; it maintains it once formed. Thus, when VE-Cadherin is downregulated, cells part and permeability increases (8). Notably, VEGF is known to promote vascular leakage, and apparently does so by inducing a beta -arrestin-dependent endocytosis of VE-Cadherin (9). Part of this effect may be mediated by VE-Cadherin itself which is reported to increase the membrane half-life of VEGFR2 (10). VE-Cadherin acts homotypically at sites of zonula adherens. On each expressing cell, it is proposed that VE-Cadherin first forms a trimer, which then dimerizes with a trimeric counterpart in-trans. Alternatively, two cis-dimers could act in-trans to generate homotypic binding (11). In addition to cell adhesion, VE-Cadherin also is reported to mediate TGF-beta receptor assembly. When clustered, VE-Cadherin enhances T beta RII/T beta RI assembly into an active receptor complex on endothelial cells (12). VE-Cadherin is expressed on endothelial cells, trophoblast cells, endothelial progenitor cells and embryonic hematopoietic cells (5, 8, 13, 14).

  1. Patel, S.D. et al. (2007) Curr. Opin. Struct. Biol. 13:690.
  2. Vestweber, D. (2008) Arterioscler. Thromb. Vasc. Biol. 28:223.
  3. Vincent, P.A. et al. (2004) Am. J. Physiol. Cell. Physiol. 286:C987.
  4. Cavallaro, U. et al. (2006) Exp. Cell Res. 312:659.
  5. Breier, G. et al. (1996) Blood 87:630.
  6. Huber, P. et al. (1996) Genomics 32:21.
  7. Pokutta, S. and W.I. Weis (2007) Annu. Rev. Cell Dev. Biol. 23:237.
  8. Crosby, C.V. et al. (2005) Blood 105:2771.
  9. Gavard, J. and J.S. Gutkind (2006) Nat. Cell Biol. 8:1223.
  10. Calera, M.R. et al. (2004) Exp. Cell Res. 300:248.
  11. Hewat, E.A. et al. (2007) J. Mol. Biol. 365:744.
  12. Rudini, N. et al. (2008) EMBO J. 27:993.
  13. Kogata, N. et al. (2006) Circ. Res. 98:897.
  14. Ema, M. et al. (2006) Blood 108:4018.

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Bioinformatics

Gene Symbol Cdh5
Entrez
Uniprot