Recombinant Human Cadherin-8 (CAD-8) Fc Chimera Protein, CF
Recombinant Human Cadherin-8 (CAD-8) Fc Chimera Protein, CF Summary
Product Specifications
Optimal dilutions should be determined by each laboratory for each application.
| Human Cadherin-8 (Ala23-Met614) Accession # AAA35628 |
IEGRMD | Human IgG1 (Pro100-Lys330) |
6-His tag |
| N-terminus | C-terminus | ||
Analysis
Product Datasheets
Carrier Free
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.
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.
188-C8
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile 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.
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Reconstitution Calculator
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.
- Tanihara, H. et al. (1994) Cell Adhes. Comm. 2:15.
- Suzuki, S. et al. (1991) Cell Regul. 2:261.
- Nollet, F. et al. (2000) J. Mol. Biol. 299:551.
- Yamagata, K. et al. (1999) J. Biol. Chem. 274:19473.
- Kido, M. et al. (1998) Genomics 48:186.
FAQs
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