Recombinant Human LRRTM2 Fc Chimera Protein, CF

When Recombinant Rat Neurexin 1 alpha (-S4) is coated at 1 μg/mL (100 μL/well), Recombinant Human LRRTM-2 Fc Chimera (Catalog # 5589-LR) binds with an ED50 of 0.07‑0.42 μg/mL

2 μg/lane of Recombinant Human LRRTM2 was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 83-100 kDa and 160-200 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human LRRTM2 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Rat Neurexin 1 alpha (-S4) is immobilized at 1 µg/mL (100 µL/well), the concentration of Recombinant Human LRRTM2 Fc Chimera that produces 50% of the optimal binding response is 0.07-0.42 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human LRRTM2 protein
  

  Human LRRTM2 (Cys34-Arg422) Accession # O43300	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: O43300
• N-terminal Sequence: Cys34
• 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

• Dilutions:
  • Bioactivity
• Theoretical MW: 71 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: 83-100 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 °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 LRRTM2 Fc Chimera Protein, CF

• leucine-rich repeat transmembrane neuronal protein 2
• leucine rich repeat transmembrane neuronal 2
• LRRN2
• LRRTM2

Background

LRRTM2 (Leucine-rich repeat transmembrane protein 2) is a member of the LRRTM family of molecules (1). All LRRTMs are type I transmembrane proteins that contain multiple leucine rich repeats and one PDZ consensus cytoplasmic binding domain. The LRRTM family is expressed in the central nervous system across vertebrate species, and they are not found in invertebrates (1). Human LRRTM2 is synthesized as a 516 amino acid (aa) precursor that contains a 33 aa signal sequence, a 389 aa extracellular domain, a 21 aa transmembrane segment, and a 73 aa cytoplasmic region (1). The extracellular domain is characterized by the presence of ten Leucine-rich repeats, flanked by two cysteine-rich sequences. Mature human LRRTM2 is 98% aa identical to mouse LRRTM2 (1). LRRTM2 functions as a postsynaptic organizer in excitatory synapses. LRRTM2 binds only Neurexin-alpha and Neurexin-beta which are lacking splice site 4 (S4) (2). Crystal structure shows dependence of this interaction on Calcium ion as well as overlapping binding interface with Neuroligins (3). LRRTM2 is essential for long term potentiation in hippocampal neuron by maintaining AMPA Receptors at the synapse (4).

1. Lauren, J. et al. (2003) Genomics 81:411.
2. Ko, J. et al. (2009) Neuron 64:791.
3. Yamagata, A. et al. (2018) Nat. Commun. 9:3964.
4. Soler-Llavina, G.J. et al. (2013) Neuron 79:439.

Bioinformatics

• Uniprot:
  • O43300()