Recombinant Human Cadherin-13 (CAD-13) Protein, CF

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Recombinant Human Cadherin-13 (CAD-13) Protein, CF Summary

Product Specifications

>90%, 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.
Measured by the ability of the immobilized protein to inhibit the adhesion of HUVEC human umbilical vein endothelial cells. When 5 x 104 cells/well are added to rhCadherin-13 coated plates, cell adhesion is inhibited in a dose dependent manner after 2 hours at 37 °C. The ED50 for this effect is 2-8 μg/mL.
Mouse myeloma cell line, NS0-derived human Cadherin-13 protein
Glu23-Ala692, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
74.5 kDa
100-115 kDa, reducing conditions

Product Datasheets

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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.


Formulation Lyophilized from a 0.2 μm filtered solution in MES and NaCl.
Reconstitution Reconstitute at 200 μg/mL in 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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Background: Cadherin-13

Cadherin-13, also known as T-Cadherin and H‑Cadherin, is a GPI-anchored protein belonging to the Cadherin superfamily of calcium-dependent adhesion molecules. Cadherins are involved in multiple processes including embryonic development, cell migration, and maintenance of epithelial integrity (1, 2). Following removal of its C‑terminal propeptide, Cadherin-13 is expressed on the cell surface both with and without its N-terminal propeptide in species of approximately 120 kDa and 100 kDa, respectively (3). Human Cadherin-13 contains five tandem Cadherin repeats and shares 95% aa sequence identity with mouse and rat Cadherin-13 (4). It is most highly expressed in the circulatory and nervous systems, particularly on cardiac myocytes, vascular endothelial and smooth muscle cells, and neurons and astrocytes in the brain (3, 5 - 9). Cadherin-13 exerts a negative influence on neurite extension, and it is down‑regulated in neurons upon NGF stimulation (10, 11). Homotypic Cadherin-13 interactions promote intercellular adhesion which can be inhibited by its binding to LDL (12). Cadherin-13 also mediates the cardioprotective effects of Adiponectin by directly binding Adiponectin (selectively the hexameric and HMW forms) and trapping it on vascular endothelial cells and cardiomyocytes (6 ‑ 8). The role of Cadherin-13 in the vasculature is complex. When expressed on vascular endothelial cells it promotes angiogenesis, but when expressed on stromal cells it inhibits neovascularization (13, 14). Its down‑regulation on breast carcinoma cells and up‑regulation on the vasculature of various tumors limits tumor cell proliferation and angiogenesis but also enhances tumor progression (4, 8, 15).

  1. Pokutta, S. and W.I. Weis (2007) Annu. Rev. Cell Dev. Biol. 23:237.
  2. Philippova, M. et al. (2009) Cell. Signal. 21:1035.
  3. Stambolsky, D.V. et al. (1999) Biochim. Biophys. Acta 1416:155.
  4. Lee, S.W. (1996) Nat. Med. 2:776.
  5. Doyle, D.D. et al. (1998) J. Biol. Chem. 273:6937.
  6. Denzel, M.S. et al. (2010) J. Clin. Invest. 120:4342.
  7. Hug, C. et al. (2004) Proc. Natl. Acad. Sci. 101:10308.
  8. Hebbard, L.W. et al. (2008) Cancer Res. 68:1407.
  9. Takeuchi, T. et al. (2000) J. Neurochem. 74:1489.
  10. Fredette, B.J. et al. (1996) Development 122:3163.
  11. Bai, S. et al. (2007) J. Biol. Chem. 282:27171.
  12. Resink, T.J. et al. (1999) FEBS Lett. 463:29.
  13. Philippova, M. et al. (2006) Arterioscler. Thromb. Vasc. Biol. 26:2222.
  14. Rubina, K. et al. (2007) Angiogenesis 10:183.
  15. Wyder, L. et al. (2000) Cancer Res. 60:4682.
Entrez Gene IDs
1012 (Human); 12554 (Mouse); 192248 (Rat)
Alternate Names
cadherin 13, H-cadherin (heart); Cadherin13; Cadherin-13; CDH13; CDHHT-cadherin; H-Cadherin; Heart cadherin; heart-cadherin; P105; T-cad; T-Cadherin; Truncated cadherin; truncated-cadherin


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