Recombinant Human LRFN5 Fc Chimera Protein, CF
Recombinant Human LRFN5 Fc Chimera Protein, CF Summary
|Human LRFN5 |
Accession # Q96NI6
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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).
- Morimura, N. et al. (2006) Gene 380:72.
- Wang, C.-Y. et al. (2006) J. Neurosci. 26:2174.
- Wang, P.Y. et al. (2008) Mol. Cell. Neurosci. 39:83.
- Yuwen, Z. et al. (2106) Sci Adv. Apr;2(4).
- Choi, Y. et al. (2016) Sci Adv. Apr; 2(4).
- de Bruijn D.R.H. et al. (2010) Mol Syndromol 46.
- Xu, B. et al. (2009) PNAS 106:16746.
- Choi, Y. et.al. (2016) Sci Rep. 6:26676.
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