Recombinant Human LINGO-1 Protein, CF

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When BiotinylatedRecombinant Human Nogo Receptor Fc Chimera is present at 2.5 μg/mL, Recombinant Human LINGO‑1 (Catalog # 9737‑LG) binds with anED50 of 0.4‑2.4 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human LINGO-1 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Biotinylated Recombinant Human Nogo Receptor Fc Chimera is present at 2.5 μg/mL, the concentration of Recombinant Human LINGO-1 that produces 50% of the optimal binding response is 0.4-2.4 μg/mL.  
Source
Human embryonic kidney cell, HEK293-derived human LINGO-1 protein
Thr40-Thr556, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Thr40
Protein/Peptide Type
Recombinant Proteins
Purity
>80%, 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

Dilutions
  • Bioactivity
Theoretical MW
60 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
82-112 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 °C as supplied.
  • 2 weeks, 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 with Trehalose.
Purity
>80%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 1 mg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human LINGO-1 Protein, CF

  • FLJ14594
  • LERN1
  • LERN1UNQ201
  • leucine rich repeat and Ig domain containing 1
  • leucine rich repeat neuronal 6A
  • Leucine-rich repeat and immunoglobilin domain-containing protein 1
  • Leucine-rich repeat neuronal protein 1
  • Leucine-rich repeat neuronal protein 6A
  • LINGO1
  • LINGO-1
  • LRRN6A
  • LRRN6Aleucine-rich repeat neuronal 6A
  • MGC17422

Background

LINGO-1 (Leucine-rich repeat and immunoglobulin-like domain-containing Nogo receptor-interacting protein 1), also known as LERN1 (Leucin-rich repeat neuronal protein 1) or LRRN6A (Leucine-rich repeat neuronal protein 6A), is a 614 amino acid (aa) transmembrane protein of the leucine-rich repeat (LRR) family, ribonuclease inhibitor subfamily (1). The four known LINGO proteins (LINGO-1, -2, -3 and -4) contain LRR and IgCAM domains in the extracellular portion and share 44‑61% aa identity (2). LINGO-1 is restricted to the nervous system and is concentrated in the brain as a component of the NgR1/p75 and NgR1/Taj (TROY) signaling complexes (3). LINGO-1 negatively regulates neurite outgrowth and myelination. LINGO-1 is highly conserved, showing 99% aa identity between human, mouse and rat (2, 4). LINGO-1 promotes lysosomal degradation of amyloid-beta protein precursor and acts as a key player in Alzheimer's Disease progression (5). It suppresses oligodendrocyte precursor cell and myelin maturation, which leads to neurodegeneration (6). The intracellular LINGO-1 negatively regulates Trk receptors' signaling by modulating their lysosomal degradation (7). Inhibition of LINGO-1 may protect against degeneration of dopamine neurons in Parkinson's disease (8).
  1. Mosyak, L. et al. (2006) J. Biol. Chem. 281:36378.
  2. Mi, S. et al. (2004) Nat. Neurosci. 7:221.
  3. Fernandez-Enright, F. et al. (2014) Transl. Psychiatry. 4:e348.
  4. Mi, S. (2008) Cytokine Growth Factor Rev. 19:245.
  5. de Laat, R. et al. (2015) Pathobiol. Aging Age Relat. Dis. 5:25796.
  6. Foale, S. et al. (2017) Neural. Regen. Res. 12:1247.
  7. Meabon, J.S. et al. (2016) Mol. Cell Neurosci. 70:1.
  8. Inoue, H. et al. (2007) Proc. Natl. Acad. Sci. U.S.A. 104:14430.

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