• Species Reactivity

  Mouse

• Specificity

  Detects mouse VE-Cadherin in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant human (rh) Cadherin-8, rhCadherin-17, rhN-Cadherin, recombinant mouse (rm) E-Cadherin, or rmP-Cadherin is observed.

• Source

  Monoclonal Rat IgG2b Clone # 162709

• Immunogen

  Mouse myeloma cell line NS0-derived recombinant mouse VE-Cadherin    
  Asp46-Gln592 (Gly67 del, Ile69Asp, Lys70Gln)    
  Accession # 2208309A

• Formulation

  Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

• Label

  Alexa Fluor 700

Applications

• 
  

  Recommended    
  Concentration

  Sample

• Flow Cytometry

  0.25-1 µg/10    ⁶ cells

  bEnd.3 mouse endothelioma cell line

• 
  

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

Preparation and Storage

• Shipping

  The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

• Stability & Storage

  Store the unopened product at 2 - 8 °C. Do not use past expiration date.

Background: VE-Cadherin

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 (1-4). Subfamilies include classical/type I, atypical/type II, and desmosomal-related cadherins (1-3). 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 VEGF R2 (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).

• References:

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.

• 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