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Recombinant Human Cadherin-8 (CAD-8) Fc Chimera Protein, CF

Catalog # 188-C8 | R&D Systems, Inc. a Bio-Techne Brand
Catalog #
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Key Product Details



Accession #

Structure / Form

Disulfide-linked homodimer





Product Specifications


Mouse myeloma cell line, NS0-derived human Cadherin-8 protein
Human Cadherin-8
Accession # AAA35628
6-His tag
N-terminus C-terminus


>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.

N-terminal Sequence Analysis


Predicted Molecular Mass

93 kDa (monomer)


105-158 kDa, reducing conditions


Measured by the ability of the immobilized protein to support the adhesion of Caki‑2 human clear cell carcinoma epithelial cells.
When 5 x 104 cells/well are added to Recombinant Human Cadherin‑8 Fc Chimera coated plates (5 µg/mL with 100 µL/well), approximately >30% will adhere after 30 minutes at 37 °C.
Optimal dilutions should be determined by each laboratory for each application.

Formulation, Preparation and Storage

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitute at 100 μg/mL in sterile PBS.

Reconstitution Buffer Available:
Size / Price
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.

Background: Cadherin-8

Cadherin-8 is a member of the type II, also called atypical, subfamily of classic cadherin cell adhesion molecules. Cadherins are transmembrane calcium-dependent cell adhesion proteins. On their cytoplasmic side, they associate with the three catenins, alpha, beta and gamma (plakoglobin). This association links the cadherin protein to the cytoskeleton. Type I cadherins consist of a large extracellular domain with an N-terminal propeptide sequence that is proteolytically cleaved intracellularly, five cadherin repeats and four calcium-binding pockets between the cadherin repeats a single-pass transmembrane domain, and a short carboxy-terminal cytoplasmic domain responsible for interacting with the catenins. Within the N-terminal cadherin domain, a conserved HAV motif involved in homophilic interaction is present. In contrast, the type II cadherins do not contain the HAV motif in the N-terminal cadherin domain and display weak or no cell adhesive properties. There also appears to be more diversity in the cytoplasmic domains of the type II cadherins as compared to the type I cadherins. Cadherin-8 is most highly expressed in neuronal tissues. The rat Cadherin-8 protein has been suggested to play a role in long-term potentiation. Human Cadherin-8 is a 799 amino acid (aa) residue protein with a putative 29 aa signal sequence, and a 32 aa propeptide, a 560 aa mature extracellular domain, a 21 aa transmembrane domain and a 157 aa cytoplasmic domain. The human, mouse and rat proteins share approximately 98% homology.


  1. Tanihara, H. et al. (1994) Cell Adhes. Comm. 2:15.
  2. Suzuki, S. et al. (1991) Cell Regul. 2:261.
  3. Nollet, F. et al. (2000) J. Mol. Biol. 299:551.
  4. Yamagata, K. et al. (1999) J. Biol. Chem. 274:19473.
  5. Kido, M. et al. (1998) Genomics 48:186.

Alternate Names

Cadherin8, CDH8

Entrez Gene IDs

1006 (Human)

Gene Symbol



Product Documents for Recombinant Human Cadherin-8 (CAD-8) Fc Chimera Protein, CF

Certificate of Analysis

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Product Specific Notices for Recombinant Human Cadherin-8 (CAD-8) Fc Chimera Protein, CF

For research use only

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