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Recombinant Human N-Cadherin Fc Chimera Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 1388-NC

Analyzed by SEC-MALS
R&D Systems, part of Bio-Techne
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1388-NC-050

Key Product Details

Source

NS0

Accession #

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

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

Purity

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Asp160

Predicted Molecular Mass

89.2 kDa (monomer)

SDS-PAGE

115‑130 kDa, reducing conditions

Activity

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.

Scientific Data Images for Recombinant Human N-Cadherin Fc Chimera Protein, CF

Recombinant Human N‑Cadherin Fc Chimera Protein SEC-MALS.

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 post-translational modifications (PTMs) present (i.e. Glycosylation).

Formulation, Preparation and Storage

1388-NC
Formulation Lyophilized from a 0.2 μm filtered solution in Tris-Citrate.
Reconstitution
Reconstitute at 100 μg/mL in sterile, deionized water containing 2 mM calcium 24 hours prior to use.

Reconstitution Buffer Available:
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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.
  • 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.

Background: N-Cadherin

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).

References

  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.

Long Name

Neural Cadherin

Alternate Names

Cadherin-2, CD325, CDH2, NCadherin

Entrez Gene IDs

1000 (Human); 12558 (Mouse); 83501 (Rat)

Gene Symbol

CDH2

UniProt

Additional N-Cadherin Products

Product Documents for Recombinant Human N-Cadherin Fc Chimera Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human N-Cadherin Fc Chimera Protein, CF

For research use only

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