Recombinant Human E-Cadherin Fc Chimera Protein, CF

Recombinant Human E-Cadherin Fc Chimera Protein (Catalog # 11525-EC) supports the adhesion of the MCF-7 human breast cancer cells. The ED50 for this effect is 0.100-1.50 μg/mL.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human E-Cadherin Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of the MCF‑7 human breast cancer cells. The ED₅₀ for this effect is 0.100-1.50 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human E-Cadherin protein
  

  Human ECAD (Asp 155-Ile 707) Accession # P12830.3	GGIEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: P12830.3
• N-terminal Sequence: Asp155
• Structure / Form:

  Disulfide-linked homodimer

• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 87 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: 100-114 kDa, under 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 with Trehalose.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 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 E-Cadherin Fc Chimera Protein, CF

• Arc-1
• CAD1
• cadherin 1, E-cadherin (epithelial)
• cadherin 1, type 1, E-cadherin (epithelial)
• Cadherin-1
• calcium-dependent adhesion protein, epithelial
• CAM 120/80
• CD324 antigen
• CD324
• CDH1
• CDHE
• cell-CAM 120/80
• Cell-CAM120/80
• ECAD
• ECadherin
• E-Cadherin
• Epithelial cadherin
• LCAM
• L-CAM
• UVOE-Cadherin
• Uvomorulin

Background

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). Human E-Cadherin shares 81% amino acid sequence identity with the rat and mouse proteins (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 N-terminal domain can be cleaved by several proteases and is released as a soluble factor that enhances cancer cell motility and EGFR-dependent survival and proliferation (6).

1. Gumbiner, B.M. (2005) Nat. Rev. Mol. Cell Biol. 6:622.
2. Bussemakers, M.J. et al. (1993) Mol. Biol. Rep. 17:123.
3. Guillot, C. and T. Lecuit (2013) Science 340:1185.
4. Tian, X. et al. (2011) J. Biomed. Biotechnol. 2011:567305.
5. Stemmler, M.P. (2008) Mol. Biosyst. 4:835.
6. David, J.M. and A.K. Rajasekaran (2012) Cancer Res. 72:2917.

Bioinformatics

• Uniprot:
  • P12830.3()