Recombinant Human N-Cadherin Fc Chimera Protein, CF

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Recombinant Human N-Cadherin Fc Chimera (Catalog # 1388-NC) has a molecular weight (MW) of 244.7 kDa as analyzed by SEC-MALS, suggesting that this protein is a homodimer.  MW may differ from predicted MW due to ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free
Datasheet
Reviews & Publications
Protocols & FAQs
Support & Research

Recombinant Human N-Cadherin Fc Chimera Protein, CF Summary

Additional Information
Analyzed by SEC-MALS
Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of U‑118‑MG human glioblastoma/astrocytoma cells. Recombinant Human N-Cadherin Fc Chimera immobilized at 10 µg/mL, 100 µL/well, will induce  ≥55% cell adhesion.
Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human N-Cadherin protein
Human N-Cadherin
Asp160-Ala724
Accession # P19022.4
IEGRMD Human IgG1
(Pro100-Lys330)
6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Asp160
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
CDH2
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
89.2 kDa (monomer).
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
115‑130 kDa, reducing conditions
Publications
Read Publications using
1388-NC in the following applications:

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 Tris-Citrate.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile, deionized water containing 2 mM calcium 24 hours prior to use.

Notes

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

Alternate Names for Recombinant Human N-Cadherin Fc Chimera Protein, CF

  • ACOGS
  • ARVD14
  • cadherin 2, type 1, N-cadherin (neuronal)
  • Cadherin-2
  • calcium-dependent adhesion protein, neuronal
  • CD325 antigen
  • CD325
  • CDH2
  • CDHN
  • CDw325
  • NCAD
  • N-cadherin 1
  • NCadherin
  • N-Cadherin
  • Neural cadherin
  • neural-cadherin

Background

Neuronal Cadherin (N-Cadherin or NCAD), also known as Cadherin-2 (CDH2), is a 130 kDa type I membrane 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 N‑Cadherin is synthesized with a 25 amino acid (aa) signal peptide and a 134 aa N‑terminal propeptide. The mature cell surface‑expressed protein consists of a 565 amino acid (aa) extracellular domain (ECD) that contains five Cadherin repeats, a 21 aa transmembrane segment, and a 161 aa cytoplasmic domain (3). Within the ECD, human N-Cadherin shares 98% aa sequence identity with mouse and rat N-Cadherin. In the nervous system, N-Cadherin mediates adhesion between the opposing faces of developing neuronal synapses and between Schwann cells and neuronal axons (4, 5). It interacts in cis or in trans homophilically and with the GluR2 subunit of neuronal AMPA receptors (1, 6). During synaptic maturation, its expression is lost from inhibitory terminals but maintained at excitatory terminals (5). ADAM10-mediated shedding of the N-Cadherin ECD alters cell-cell adhesion, synaptic development, and AMPA receptor activity (7, 8). N-Cadherin can also be cleaved at multiple additional sites within the intracellular or extracellular domains by Calpain, gamma ‑Secretase, and several MMPs (9-13). Cleavage of N‑Cadherin in atherosclerotic plaques contributes alternatively to vascular smooth muscle cell proliferation (MMP-9 and -12) or apoptosis
(MMP‑7) (12, 13). Aberrant cell surface expression of the pro and mature forms of N-Cadherin in cancer results in increased tumor progression and invasiveness (14, 15). N-Cadherin also mediates the adhesion between hematopoeitic progenitor cells and mesenchymal stromal cells of the bone marrow (16).
  1. Pokutta, S. and W.I. Weis (2007) Annu. Rev. Cell Dev. Biol. 23:237.
  2. Gumbiner, B.M. (2005) Nat. Rev. Mol. Cell Biol. 6:622.
  3. Reid, R.A. and J.J. Hemperly (1990) Nucleic Acids Res. 18:5896.
  4. Wanner, I.B. and P.M. Wood (2002) J. Neurosci. 22:4066.
  5. Benson, D.L. and H. Tanaka (1998) J. Neurosci. 18:6892.
  6. Saglietti, L. et al. (2007) Neuron 54:461.
  7. Reiss, K. et al. (2005) EMBO J. 24:742.
  8. Malinverno, M. et al. (2010) J. Neurosci. 30:16343.
  9. Jang, Y.-N. et al. (2009) J. Neurosci. 29:5974.
  10. Uemura, K. et al. (2006) Neurosci. Lett. 402:278.
  11. Hartland, S.N. et al. (2009) Liver Int. 29:966.
  12. Williams, H. et al. (2010) Cardiovasc. Res. 87:137.
  13. Dwivedi, A. et al. (2009) Cardiovasc. Res. 81:178.
  14. Maret, D. et al. (2010) Neoplasia 12:1066.
  15. Tanaka, H. et al. (2010) Nat. Med. 16:1414.
  16. Wein, F. et al. (2010) Stem Cell Res. 4:129.

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Bioinformatics

Gene Symbol CDH2
Uniprot