Recombinant Mouse Contactin-1 Protein, CF

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When Recombinant Mouse Contactin‑1 (Catalog # 9665‑CN) is immobilized at 1 µg/mL(100 µL/well), Recombinant Human NrCAM Fc Chimera (Catalog # 2034‑NR) binds with an ED50 of 0.03‑0.18 μg/mL.

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse Contactin-1 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Contactin‑1 is coated at 1 µg/mL, 100 μL/well, Recombinant Human NrCAM Fc Chimera (Catalog # 2034-NR) binds with an ED50 of 0.03-0.18 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Contactin-1 protein
Mouse Contactin-1
(Asp21-Thr999)
Accession # AAH66864
HPGGGSGGGSGGGS HHHHHH
N-terminusC-terminus
Accession #
N-terminal Sequence
Asp21
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, 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

Theoretical MW
111 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
119-135 kDa, 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.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 400 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 Mouse Contactin-1 Protein, CF

  • CNTN1
  • contactin 1
  • Contactin1
  • Contactin-1
  • F11
  • F3
  • F3cam
  • Glycoprotein gp135
  • GP135
  • Neural cell surface protein F3

Background

Contactin-1 (CNTN1), also known as F3 and F11, is an approximately 135 kDa GPI-anchored member of the Contactin family of neuronal adhesion glycoproteins (1). Mature mouse Contactin-1 contains 6 Ig-like domains and 4 fibronectin type III-like domains, and it shares 96% and 100% amino acid (aa) sequence identity with human and rat Contactin-1, respectively (2, 3). Alternative splicing generates an isoform with an 11 aa deletion N-terminal to the first Ig-like domain and another isoform that is substituted and truncated following the sixth Ig-like domain. In humans, Contactin-1 is critical in the development of the central nervous system, and a soluble form of Contactin-1 is released into the cerebrospinal fluid (4). Contactin-1 is expressed on neurons and their precursors at sites of glial cell contact with neuronal processes (5-7). Within paranodal regions of the axon, Contactin-1 associates in cis with the transmembrane protein Caspr (7). It binds in trans to other neuronal adhesion proteins (e.g. NrCAM, Neurofascin, Tenascin R), the phosphatase PTPRZ, and the chondroitin sulfate CS-E (8-13). It also binds and activates both Notch-1 and Notch-2 (14). In cancer, Contactin-1 is up-regulated by VEGF-C and is required for VEGF R3/Flt-4 induced tumor cell invasion and metastasis (15). In humans, mutations in CNTN1 cause a familial form of lethal congenital myopathy (16).
  1.  Shimoda, Y. and K. Watanabe (2009) Cell Adh. Migr. 3:64.
  2. Reid, R.A. et al. (1994) Brain Res. Mol. Brain Res. 21:1.
  3. Berglund, E.O. and B. Ranscht (1994) Genomics 21:571.
  4. Durbec, P. et al. (1992) J. Cell Biol. 117:877.
  5. Gennarini, G. et al. (1990) Acta Histochem. 38:65.
  6. Bizzoca, A. et al. (2012) Dev. Biol. 365:133.
  7. Boyle, M.E.T. et al. (2001) Neuron 30:385.
  8. Volkmer, H. et al. (1996) J. Cell Biol. 135:1059.
  9. Xenaki, D. et al. (2011) Development 138:519.
  10. Volkmer, H. et al. (1998) J. Cell Biol. 142:1083.
  11. Pesheva, P. et al. (1993) Neuron 10:69.
  12. Peles, E. et al. (1995) Cell 82:251.
  13. Mikami, T. et al. (2009) J. Biol. Chem. 284:4494.
  14. Hu, Q.-D. et al. (2003) Cell 115:163.
  15. Su, J.-L. et al. (2006) Cancer Cell 9:209.
  16. Compton AG (2008) Am J Hum Genet 83:714.

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