Recombinant Human Cadherin-7 (CAD-7) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Cadherin-7 (CAD-7) Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of U‑87 MG human glioblastoma/astrocytoma cells.

The ED50 for this effect is 1.0-4.0 μg/mL.

Optimal dilutions should be determined by each laboratory for each application.

Source
Chinese Hamster Ovary cell line, CHO-derived human Cadherin-7 protein
Met1-Thr607, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser48
Protein/Peptide Type
Recombinant Proteins
Gene
CDH7
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
62.2 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
80 - 90 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 200 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 Human Cadherin-7 (CAD-7) Protein, CF

  • CAD7
  • cadherin 7, type 2
  • Cadherin7
  • Cadherin-7
  • CDH7
  • CDH7L1

Background

Cadherin-7 is an approximately 115 kDa type I transmembrane 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). Human Cadherin-7 is synthesized with a 27 amino acid (aa) signal peptide and a 20 aa N-terminal propeptide. The mature cell surface-expressed protein consists of a 738 amino acid (aa) extracellular domain (ECD) that contains five Cadherin repeats, a 21 aa transmembrane segment, and a 157 aa cytoplasmic domain (2, 3). Within the ECD, human Cadherin-7 shares 99% and 97% aa sequence identity with mouse and rat Cadherin-7, respectively. Cadherin-7 interacts homotypically and heterotypically with Cadherin-14 and more weakly with Cadherins-6, -9, and -12 (3, 4). Cellular adhesion mediated by Cadherin-7 is more weak than that mediated by E- or N-Cadherin, although it can be strengthed by Fibronectin binding to Integrins on the same cell (5, 6). Cadherin-7 is localized to discrete regions of the developing nervous system. In chick and mouse, it is expressed in the basal plate of the neural tube, migrating cranial motoneurons, and migrating neural crest cells (4, 7, 8), lateral regions of the hindbrain and migrating Purkinje cell precursors (8, 9), striatum, parahippocampal areas, and somatosensory cortex of the forebrain (10 - 12), neural retina and cochlea (13, 14). Cadherin-7 interactions promote motor axon growth and inhibit axonal branching, whereas Cadherin-6B promotes branching during cranial motorneuron development (7). Cadherin-7 performs a similar function during limb bud development during which it participates in the migration and condensation of mesenchymal cells (15). Cadherin-7 is overexpressed on primary melanoma cells where it binds melanoma inhibitory activity (MIA), a secreted melanoma cell protein that promotes tumor progression (16).
  1. Pokutta, S. and W.I. Weis (2007) Annu. Rev. Cell Dev. Biol. 23:237.
  2. Kools, P. et al. (2000) Genomics 68:283.
  3. Shimoyama, Y. et al. (2000) Biochem. J. 349:159.
  4. Nakagawa, S. et al. (1995) Development 121:1321.
  5. Chu, Y.-S. et al. (2006) J. Biol. Chem. 281:2901.
  6. Martinez-Rico, C. et al. (2009) J. Cell Sci. 123:712.
  7. Barnes, S.H. et al. (2010) Development 137:805.
  8. Ju, M.J. et al. (2004) Neuroscience 128:785.
  9. Luo, J. et al. (2004) Mol. Cell. Neurosci. 25:138.
  10. Redies, C. et al. (2002) Brain Res. Bull. 57:489.
  11. Kovjanic, D. and C. Redies (2003) J. Comp. Neurol. 456:95.
  12. Krishna-K, K. et al. (2011) Neuroscience 175:37.
  13. Faulkner-Jones, B.E. et al. (1999) Mol. Cell. Neurosci. 14:1.
  14. Luo, J. et al. (2007) Dev. Dyn. 236:2331.
  15. Kim, D. et al. (2009) J. Cell. Physiol. 221:161.
  16. Winklmeier, A. et al. (2009) Cancer Sci. 100:261.

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Bioinformatics

Gene Symbol CDH7
Uniprot