Recombinant Human P-Cadherin Fc Chimera Avi-tag Protein, CF

Biotinylated Recombinant Human P-Cadherin Fc Chimera Avi-tag Protein (Catalog # AVI11651) binds Recombinant Human CDCP1 Fc Chimera (10402-CU) with an ED50 of 0.500-7.00 μg/mL.

2 μg/lane of Biotinylated Recombinant Human P‑Cadherin Fc Chimera Avi-tag Protein (Catalog # AVI11651) was resolved with SDS-PAGE under reducing (R) condition and visualized by Coomassie® Blue staining, showing bands at 103-130 kDa.

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

Recombinant Human P-Cadherin Fc Chimera Avi-tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human P-Cadherin Fc Chimera Avi-tag (Catalog # AVI11651) binds Recombinant Human CDCP1 Fc Chimera (Catalog # 10402-CU) with an ED₅₀ of 0.500-7.00 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human P-Cadherin protein
  

  Human PCAD (Asp108-Gly654) Accession # CAA45177.1	IEGRMDGG	Human IgG1 (Pro100-Lys330)	Avi-tag
  N-terminus			C-terminus

• N-terminal Sequence: Asp108
• Structure / Form: Disulfide linked homodimer
  Biotinylated via Avi-tag
• Protein/Peptide Type: Recombinant Proteins
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 88 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: 103-130 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.
• Reconstitution Instructions: Reconstitute at 200 μg/mL in water.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human P-Cadherin Fc Chimera Avi-tag Protein, CF

• CAD3
• cadherin 3, P-cadherin (placental)
• cadherin 3, type 1, P-cadherin (placental)
• Cadherin-3
• CDH3
• CDHP
• CDHPcalcium-dependent adhesion protein, placental
• HJMD
• PCAD
• PCadherin
• P-Cadherin
• PCADP-cadherin
• Placental cadherin

Background

Placental (P) - Cadherin (PCAD) is a member of the Cadherin family of cell adhesion molecules. Cadherins are calcium-dependent transmembrane proteins, which bind to one another in a homophilic manner. On their cytoplasmic side, they associate with the three catenins, alpha , beta , and gamma (plakoglobin). This association links the cadherin protein to the cytoskeleton. Without association with the catenins, the cadherins are non-adhesive. Cadherins play a role in development, specifically in tissue formation. They may also help to maintain tissue architecture in the adult. P-Cadherin is a classical cadherin molecule. Classical cadherins consist of a large extracellular domain which contains DXD and DXNDN repeats responsible for mediating calcium-dependent adhesion, a single-pass transmembrane domain, and a short carboxy-terminal cytoplasmic domain responsible for interacting with the catenins. Human P-Cadherin is an 829 amino acid (aa) protein with a 26 aa signal sequence and an 803 aa propeptide. The mature protein begins at aa 108 and has a 548 aa extracellular region, a 23 aa transmembrane region, and a 151 aa cytoplasmic region. The human and mouse mature PCAD proteins share 87% homology. Our Avi-tag Biotinylated human P-Cadherin Fc Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

1. Shimoyama, Y. et al. (1989) J. Cell Biol. 109:1787.
2. Bussemakers, M.J.G. et al. (1993) Mol. Biol. Reports 17:123.
3. Overduin, M. et al. (1995) Science 267:386.
4. Takeichi, M. (1991) Science 251:1451.
5. Nose, A. et al. (1987) EMBO J. 6:3655.