Recombinant Human Cadherin-10 (CAD-10) Fc Chimera, CF Summary
Product Specifications
Optimal dilutions should be determined by each laboratory for each application.
Human Cadherin-10 (Glu23-Ala613) Accession # Q9Y6N8 |
IEGRMD | Human IgG1 (Pro100-Lys330) |
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.
6770-CA
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 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.
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Reconstitution Calculator
Background: Cadherin-10
Cadherin-10, also known as T2-Cadherin, is an approximately 120 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, 2). Human Cadherin-10 is synthesized with a 22 amino acid (aa) signal peptide and a 32 aa N‑terminal propeptide. The mature cell surface-expressed protein consists of a 559 amino acid (aa) extracellular domain (ECD) that contains five tandem Cadherin repeats, a 21 aa transmembrane segment, and a 154 aa cytoplasmic domain (3, 4). Within the propeptide and ECD, human Cadherin-10 shares 97% aa sequence identity with mouse and rat Cadherin-10. It interacts homotypically as well as hetertypically with Cadherin-9 and more weakly with Cadherin-6 (4). Cadherin-10 is expressed in the central nervous system, particularly in the limbic system, frontal cortex, somatosensory barrel cortex (in rat), olfactory structures, epithelial cells lining the choroid plexus and ventricles, retinal pigmented epithelium, and endothelial cells of the brain and retinal microvasculature (3, 5‑10). It is also expressed on epithelial luminal cells of the prostate, as well as in testes, ovary, placenta, kidney, small intestine, and on CD4+CD8+ T cells (3, 10‑13). Cadherin-10 expression is decreased postnatally in the barrel cortex and testes (8, 12). It is also down‑regulated in glioblastoma vasculature and prostate cancer (10, 11). Polymorphisms of human Cadherin-10 are associated with autism spectrum disorders (6).
- Pokutta, S. and W.I. Weis (2007) Annu. Rev. Cell Dev. Biol. 23:237.
- Gumbiner, B.M. (2005) Nat. Rev. Mol. Cell Biol. 6:622.
- Kools, P. et al. (1999) FEBS Lett. 452:328.
- Shimoyama, Y. et al. (2000) Biochem. J. 349:159.
- Fushimi, D. et al. (1997) Dev. Dyn. 209:269.
- Wang, K. et al. (2009) Nature 459:528.
- Bekirov, I.H. et al. (2002) Neuroscience 115:213.
- Gil, O.D. et al. (2002) J. Comp. Neurol. 453:372.
- Akins, M.R. et al. (2007) J. Comp. Neurol. 501:483.
- Williams, M.J. et al. (2005) Brain Res. 1058:62.
- Walker, M.M. et al. (2008) Mod. Pathol. 21:85.
- Munro, S.B. and O.W. Blaschuk (1996) Biol. Reprod. 55:822.
- Munro, S.B. et al. (1996) Cell. Immunol. 169:309.
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