Recombinant Human LRRN3/NLRR-3 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human LRRN3/NLRR-3 Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to enhance the adhesion of Saos‑2 human osteosarcoma cells to human Fibronectin. When 3 x 104 cells per well are added to rhNLRR-3 coated plates (5 μg/mL, 100 μL/well), approximately 50-70% will adhere after 1 hour at 37 °C.
Source
Mouse myeloma cell line, NS0-derived human LRRN3/NLRR-3 protein
Val23-Thr628, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Val23
Protein/Peptide Type
Recombinant Proteins
Gene
LRRN3
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.1 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
69.3 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
90-95 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
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile PBS,

Notes

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

Alternate Names for Recombinant Human LRRN3/NLRR-3 Protein, CF

  • FIGLER5
  • immunoglobulin and leucine rich repeat domains 5
  • leucine rich repeat neuronal 3
  • leucine-rich repeat neuronal protein 3
  • leucine-rich repeat protein, neuronal 3
  • LRRN3
  • Neuronal leucine-rich repeat protein 3
  • NLRR3
  • NLRR-3

Background

Neuronal leucine-rich repeat 3 (NLRR-3) is an 85 kDa, N-glycosylated member of a CNS-associated family of transmembrane molecules that includes AMIGO, FLRT, LINGO, LRIG, SLITRK, and Trk subgroups (1, 2). Mature human NLRR-3 consists of a 606 amino acid (aa) extracellular domain (ECD) with 13 LRRs, an RGD integrin-binding motif, one Ig-like domain, and one fibronectin type III-like domain, a 21 aa transmembrane segment, and a 59 aa cytoplasmic domain (3). Within the ECD, human NLRR-3 shares 91% aa sequence identity with mouse and rat NLRR-3. NLRR-3 is expressed in specific areas of the developing and adult CNS, and more weakly in other tissues including lung, liver, kidney, and adrenal gland (2 - 5). It is preferentially expressed in the third layer of the cerebral cortex in contrast to other NLRRs which are more diffusely distributed between cortical layers (6). During mouse development, its expression pattern is generally complementary to that of SLITRK6 in select brain regions, plus the cochlea, eye, tongue, teeth, and nasal mesenchyme (7). NLRR-3 is upregulated in the cerebral cortex following injury (3, 6). Its expression is dependent on NGF stimulation and is strongest in NGF responsive TrkA+ neuroblastoma cell lines that are weakly aggressive (3). The cytoplasmic domain of NLRR-3 contains two Yxxf motifs which are required for its clathrin-mediated internalization (8). The association of NLRR-3 with clathrin and beta -adaptin promotes the enhancement and prolongation of EGF induced signaling (8).

  1. Chen, Y. et al. (2006) Brain Res. Rev. 51:265.
  2. Haines, B.H. et al. (2005) Dev. Biol. 281:145.
  3. Hamano, S. et al. (2004) Int. J. Oncol. 24:1457.
  4. Taniguchi, H. et al. (1996) Brain Res. Mol. Brain Res. 36:45.
  5. Fukamachi, K. et al. (2001) Biochem. Biophys. Res. Commun. 287:257.
  6. Ishii, N. et al. (1996) Brain Res. Mol. Brain Res. 40:148.
  7. Aruga, J. (2003) Gene Expr. Patterns 3:727.
  8. Fukamachi, K. et al. (2002) J. Biol. Chem. 277:43549.

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Bioinformatics

Gene Symbol LRRN3
Entrez
Uniprot