Recombinant Rat E-Cadherin Fc Chimera Protein, CF Summary
Accession # Q9R0T4
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 300 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.
E-Cadherin/Cadherin-1, also known as Uvomorulin in the mouse and rat, is a 120 kDa member of the Cadherin family of cell surface glycoproteins that mediate cell adhesion (1). Rat E-Cadherin shares 92% and 81% amino acid sequence identity with the mouse and human proteins, respectively (2). It is a single-pass transmembrane protein that mediates calcium-dependent epithelial cell adhesion. E-Cadherin has five extracellular EC domains that form homophilic cis-clusters between adjacent epithelial cells and trans-clusters within the same cell. E-Cadherin clusters are critical components of adherens junctions between epithelial cells and act in the formation and maintenance of the epithelial cell barrier (3, 4). The intracellular domain of E-Cadherin binds to the Catenin cytoskeletal complex, which includes p120 Catenin, beta-Catenin, alpha-Catenin, and Vinculin. E-Cadherin expression is critical for epithelial tissue homeostasis. Decreased E-Cadherin is associated with physiological and pathological epithelial-to-mesenchymal transition and cell migration, and E-Cadherin loss contributes to cancer metastasis (5). The extracellular E-Cadherin terminal domain can be cleaved by several proteases and is released as a soluble factor that enhances cancer cell motility and EGF R‑dependent survival and proliferation (6).
- Gumbiner, B.M. (2005) Nat. Rev. Mol. Cell Biol. 6:622.
- Nagafuchi, A. et al. (1987) Nature 329:341.
- Guillot, C. and T. Lecuit (2013) Science 340:1185.
- Tian, X. et al. (2011) J. Biomed. Biotechnol. 2011:567305.
- Stemmler, M.P. (2008) Mol. Biosyst. 4:835.
- David, J.M. and A.K. Rajasekaran (2012) Cancer Res. 72:2917.
Citations for Recombinant Rat E-Cadherin Fc Chimera Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 2
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Local contractions regulate E-cadherin rigidity sensing
Authors: YA Yang, E Nguyen, GHN Sankara Na, M Heuzé, C Fu, H Yu, RM Mège, B Ladoux, MP Sheetz
Science Advances, 2022;8(4):eabk0387.
Sample Types: Whole Cells
rMCP-2, the Major Rat Mucosal Mast Cell Protease, an Analysis of Its Extended Cleavage Specificity and Its Potential Role in Regulating Intestinal Permeability by the Cleavage of Cell Adhesion and Junction Proteins.
Authors: Fu Z, Thorpe M, Hellman L
PLoS ONE, 2015;10(6):e0131720.
Sample Types: Recombinant Protein
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