Recombinant Mouse AMIGO His-tag Protein, CF

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Recombinant Mouse Amigo (Catalog # 10084-AM) inhibits IL-2 secretion by mouse T cells in the presence of anti-CD3. The ED50 for this effect is 0.1‑1 μg/mL
2 μg/lane of Recombinant Mouse AMIGO was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 49-62 kDa.

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse AMIGO His-tag Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit IL-2 secretion by mouse T cells in the presence of anti-CD3. The ED50 for this effect is 0.1-1 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse AMIGO protein
Gly28-Thr371, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Gly28
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

Dilutions
  • Bioactivity
Theoretical MW
40 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
49-62 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 °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 100 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 AMIGO His-tag Protein, CF

  • adhesion molecule with Ig-like domain 1
  • ali2
  • Alivin-2
  • AMIGO
  • AMIGO1
  • AMIGO-1
  • AMIGOamphoterin-induced protein 1
  • amphoterin-induced gene and ORF
  • KIAA1163

Background

AMIGO (Amphoterin-induced gene and ORF) is an approximately 55 kDa transmembrane cell adhesion protein. It belongs to a family of leucine‑rich repeat (LRR) containing proteins that play various roles in nervous system development and function (1). Mature mouse AMIGO consists of a 344 amino acid (aa) extracellular domain (ECD) with six tandem LRRs flanked by LRR N- and C‑terminal domains, one immunoglobulin‑like domain, a 21 aa transmembrane segment, and a 100 aa cytoplasmic domain (2). Within the ECD, mouse AMIGO shares 86% aa sequence identity with human AMIGO and 93% with rat AMIGO. AMIGO is an N‑glycosylated protein that forms homodimers by association between LRR regions (3, 4). It has homophilic and heterophilic interactions with the related AMIGO2 and AMIGO3 proteins (2). AMIGO is expressed along developing and mature neuronal fiber tracts on neurons, astrocytes, and oligodendrocytes (2, 4). It promotes the extension and branching of hippocampal and cortical neurons (2, 4). It also supports neuronal survival following apoptotic stimulation (4). AMIGO directly associates with the potassium channel Kv2.1 and enhances ion conductance through the channel (5). Kv2.1 localization and activation is regulated by phosphorylation, but phosphorylation status does not alter its interaction with AMIGO (5, 6). Our data show that AMIGO act as ligand that inhibit anti-CD3 induced IL-2 secretion on CD3+ T cells, suggesting that it may be involved in T cell suppression.


  1. de Wit, J. et al. (2011) Annu. Rev. Cell Dev. Biol. 27:697.
  2. Kuja-Panula, J. et al. (2003) J. Cell Biol. 160:963.
  3. Kajander, T. et al. (2011) J. Mol. Biol. 413:1001.
  4. Chen, Y. et al. (2012) J. Cell. Physiol. 227:2217.
  5. Peltola, M.A. et al. (2011) EMBO Rep. 12:1293.
  6. Park, K.-S. et al. (2006) Science 313:976.

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