Recombinant Mouse Contactin-2/TAG1 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Contactin-2/TAG1 Protein, CF Summary

Details of Functionality
Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Able to significantly enhance neurite outgrowth when immobilized at 6-25 μg/mL on a nitrocellulose-coated microplate.
Source
Mouse myeloma cell line, NS0-derived mouse Contactin-2/TAG1 protein
Gln31-Ser1014, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
No results obtained: Gln31 predicted
Protein/Peptide Type
Recombinant Proteins
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
108.1 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
135-145 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 opening.
Buffer
Supplied as a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain

Notes

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

Alternate Names for Recombinant Mouse Contactin-2/TAG1 Protein, CF

  • Axonal glycoprotein TAG-1
  • axonin-1 cell adhesion molecule
  • Axonin-1
  • AXT
  • CNTN2
  • contactin 2 (axonal)
  • contactin 2 (transiently expressed)
  • Contactin2
  • Contactin-2
  • DKFZp781D102
  • FLJ37193
  • MGC157722
  • TAG1
  • TAG-1
  • TAX
  • TAX1
  • TAX-1
  • TAX1FLJ42746
  • Transient axonal glycoprotein 1
  • transiently-expressed axonal glycoprotein

Background

Contactin-2 (CNTN2), also called TAG1 (transient axonal glycoprotein), TAX1 (transiently-expressed axonal glycoprotein), or axonin-1, is a 135 kDa glycosyl-phosphatidylinositol (GPI)- anchored cell adhesion molecule that belongs to the contactin subfamily within the immunoglobulin (Ig) protein superfamily (1 - 3). Mouse Contactin-2 cDNA encodes a 30 amino acid (aa) signal peptide, a 984 aa mature secreted protein with 6 Ig-like domains followed by 4 fibronectin type III-like repeats, and a 26 aa C-terminal GPI anchor pro-sequence. GPI-specific phospholipase activity can release soluble, active Contactin-2 from the membrane (2). Mature mouse Contactin-2 shares approximately 93%, 97% and 77% aa sequence identity with human, rat and chicken Contactin-2, respectively. During development, Contactin-2 is expressed by a subset of neuronal populations in the central nervous system (CNS) and peripheral nervous system (PNS), particularly during initial phases of axon outgrowth (3 - 5). Both the 135 kDa form and a 90 kDa form are also upregulated in response to CNS injury in the adult (6). Data support a role for Contactin-2 in axon pathfinding, neurite outgrowth and adhesion, especially in the CNS (3 - 6). In mature myelinated fibers, Contactin-2 is expressed by oligodendrocytes and Schwann cells, which are myelinating glial cells of the CNS and PNS, respectively (7, 8). It is enriched in the juxtaparanodal regions, where it recruits caspr2 (contactin-associated protein 2), a transmembrane neurexin involved in cell adhesion and intercellular communication (7 - 10). The axonal Contactin-2 interacts in cis with caspr2, and in trans with another Contactin-2 on the glial membrane (8). This ternary complex is required for the accumulation and organization of K+ channels in the juxtaparanodes (9).

  1. Wolfer, D. and R. J. Giger (1994) Swissprot Accession # Q61330.
  2. Hasler, T.H. et al. (1993) Eur. J. Biochem. 211:329.
  3. Karagogeos, D. (2003) Front. Biosci. 8:s1304.
  4. Liu, Y. and M.C. Halloran (2005) J. Neurosci. 25:10556.
  5. Denaxa, M. et al. (2005) Dev. Biol. 288:87.
  6. Soares, S. et al. (2005) Eur. J. Neurosci. 21:1169.
  7. Traka, M. et al. (2002) J. Neurosci. 22:3016.
  8. Poliak, S. and E. Peles (2003) Nat. Rev. Neurosci. 4:968.
  9. Traka, M. et al. (2003) J. Cell Biol. 162:1161.
  10. Poliak, S. et al. (2003) J. Cell Biol. 162:1149.

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