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

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

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

• Details of Functionality: 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 Recombinant Human Cadherin-13 (Catalog # 3264-CA) coated plates, cell adhesion is inhibited in a dose dependent manner after 2.5 hours at 37 °C. The ED₅₀ for this effect is 1.0‑5.0 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse Cadherin-13 protein
  Met1-Gly693, with a C-terminal 6-His tag
• Accession #: NP_062681
• N-terminal Sequence: Ala22
• Protein/Peptide Type: Recombinant Proteins
• Gene: Cdh13
• Purity: >95%, 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

• Dilutions:
  • Bioactivity
• Theoretical MW: 74.4 kDa.
  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 PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Mouse Cadherin-13 (CAD-13) Protein, CF

• 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

Background

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, 4). Mouse Cadherin-13 contains five tandem Cadherin repeats and shares 95% and 98% aa sequence identity with human and rat Cadherin-13, respectively (5). 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, 4, 6 - 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. Doyle, D.D. et al. (1998) J. Biol. Chem. 273:6937.
5. Wyder, L. et al. (2000) Cancer Res. 60:4682.
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. Lee, S.W. (1996) Nat. Med. 2:776.

Publications for Cadherin-13 (6768-CA)(1)

Publication using 6768-CA

• S Göddeke, B Knebel, P Fahlbusch, T Hörbelt, G Poschmann, F van de Vel, T Benninghof, H Al-Hasani, S Jacob, Y Van Nieuwe, B Lapauw, S Lehr, DM Ouwens, J Kotzka CDH13 abundance interferes with adipocyte differentiation and is a novel biomarker for adipose tissue health Int J Obes (Lond), 2018-02-21;0(0):. 2018-02-21 [PMID: 29467502] (Bioassay, Mouse)

Bioinformatics

• Gene Symbol: Cdh13
• Uniprot:
  • NP_062681()