Recombinant Human LRFN5 Fc Chimera Protein, CF

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When Recombinant Human LRFN5 Fc Chimera (Catalog # 9385-SA)is used at 1 μg/mL, 100 μL/well, Recombinant Human LAR (Catalog #9377-PF) binds with an ED50 of 1.5-9 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human LRFN5 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human LRFN5 Fc Chimera is used at 1 μg/mL, the concentration of Recombinant Human LAR that produces 50% optimal binding response is 1.5-9 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human LRFN5 protein
Human LRFN5
(Gln18-Gly527)
Accession # Q96NI6
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
No results obtained. Gln18 inferred from enzymatic pyroglutamate treatment revealing Ile19
Structure / Form
Disulfide-linked homodimer
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
83 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
90-107 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 500 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 Human LRFN5 Fc Chimera Protein, CF

  • C14orf146
  • chromosome 14 open reading frame 146
  • DKFZp686G0210
  • fibronectin type III, immunoglobulin and leucine rich repeat domains 8
  • FIGLER8
  • leucine rich repeat and fibronectin type III domain containing 5
  • leucine-rich repeat and fibronectin type-III domain-containing protein 5
  • LRFN5
  • SALM5
  • SALM5FLJ30803

Background

Synaptic adhesion-like molecule 5 (SALM5; also leucine-rich repeat and fibronectin type-III domain-containing protein 5 (LRFN5)) is an approximately 90 kDa member of the SALM family of type I transmembrane glycoproteins (1). LRFNs comprise a family of synaptic adhesion molecules consisting of five members, each containing of an extracellular domain (ECD) of six leucine-rich repeats (LRR), an IgC2-like domain, and a fibronectin type-III domain, tandemly aligned in that order (1, 2).  LRFN-3 and -5 lack a C-terminal intracellular PDZ binding domain, which is conserved among LRFN-1, 2 and 4. Mature human LRFN-5 shares 99% amino acid sequence identity with mature mouse LRFNs. LRFN-5, like the other LRFNs, promotes neurite outgrowth as well as playing a role in neuroinflammation (3, 4). LRFN-5 is expressed in the brain and is capable of inducing presynaptic differentiation (5). Reduced expression of LRFN-5 has been associated with autism spectrum disorders and schizophrenia (6, 7). LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) have been identified as novel ligands of LRFN-5 that mediates LRFN-5 dependent presynaptic differentiation in a splicing- dependent manner. LRFN-5 interacts directly with the Ig domain of LAR-RPTPs. The postsynaptic LRFN-5 promotes synapse development by trans-synaptically interacting with presynaptic  LAR-RPTPs which is important for the regulation of excitatory synaptic strength (8).
  1. Morimura, N. et al. (2006) Gene 380:72.
  2. Wang, C.-Y. et al. (2006) J. Neurosci. 26:2174.
  3. Wang, P.Y. et al. (2008) Mol. Cell. Neurosci. 39:83.
  4. Yuwen, Z. et al. (2106) Sci Adv. Apr;2(4).
  5. Choi, Y. et al. (2016) Sci Adv. Apr; 2(4).
  6. de Bruijn D.R.H. et al. (2010) Mol Syndromol 46.
  7. Xu, B. et al. (2009) PNAS 106:16746.
  8. Choi, Y. et.al. (2016) Sci Rep. 6:26676.

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