• Purity

  >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  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 (Gln18-Gly527) Accession # Q96NI6	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  No results obtained. Gln18 inferred from enzymatic pyroglutamate treatment revealing Ile19

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  83 kDa

• SDS-PAGE

  90-107 kDa, reducing conditions

Data Images

Background: LRFN5

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).

• References:

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.

• Long Name:

  Leucine-rich Repeat and Fibronectin Type III Domain Containing 5

• Entrez Gene IDs:

  145581 (Human); 238205 (Mouse); 314164 (Rat)

• Alternate Names:

  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