Recombinant Human LRRTM1 Fc Chimera Protein, CF

2 μg/lane of Recombinant Human LRRTM1 Fc Chimera (Catalog # 10372-LR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 99-109 and 190-210 kDa, respectively.

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

Recombinant Human LRRTM1 Fc Chimera Protein, CF Summary

• Details of Functionality: Bioassay data are not available.
• Source: Chinese Hamster Ovary cell line, CHO-derived human LRRTM1 protein
  

  Human LRRTM1 (Ala35-Ile425) Accession # Q86UE6.2	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q86UE6.2
• N-terminal Sequence: Ala35
• 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:

  70 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: 99-109 kDa, under 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 LRRTM1 Fc Chimera Protein, CF

• FLJ32082
• leucine rich repeat transmembrane neuronal 1
• leucine-rich repeat transmembrane neuronal 1 protein
• leucine-rich repeat transmembrane neuronal protein 1
• LRRTM1

Background

Human LRRTM1 (leucine-rich repeat transmembrane neuronal 1) is a 58-59 kDa (predicted) type I transmembrane protein, that belongs to the LRRTM family of proteins within the leucine-rich repeat (LRR) superfamily (1). It is synthesized as a precursor with a 34 amino acid (aa) signal sequence, a 393 aa luminal region, a 21 aa transmembrane region, and a 74 aa cytoplasmic region. The luminal portion of LRRTM1 contains three N-linked glycosylation sites and 10 LRRs flanked by cysteine-rich domains (1). The cytoplasmic region contains several tyrosine, serine, and threonine residues that have potential to be phosphorylated and thus to be involved in signal transduction (1). The C-terminal also contains a conserved glutamic acid-cysteine-glutamic acid-valine sequence for potential interaction with PDZ proteins (1-2). Mature human LRRTM1 is 97% aa identical to mouse LRRTM1. LRRTM1 is expressed in both developing and adult brains. It can be detected in many brain areas such the forebrain, mid brain, olfactory bulb, striatum, thalamus and cerebral cortex (3). LRRTM1 proteins are mainly localized to postsynaptic sites and bind across the synaptic cleft to its presynaptic partner neurexins lacking the splice site 4 insert (3, 4). LRRTM1 functions as a synapse organizer and plays an essential role in synapse formation and development (3, 4). Functionally, LRRTM1 may be involved in the formation of the CNS and maintenance of CNS structure and function in the adult brain (1). In addition, LRRTM1 has been shown to be a maternally suppressed gene that is associated paternally with handedness and schizophrenia (3). LRRTM1 was also reported to be associated with schizophrenia and autism spectrum disorder (5, 6).

1. Lauren, J. et al. (2003) Genomics 81:411.
2. Haines, B.P. and P.W.J. Rigby (2007) Gene Expr. Patterns 7:23.
3. Roppongi, R.T. et al. (2017) Neurosci. Res. 116:18.
4. Ko, J. (2012) Mol. Cells. 34:335.
5. Francks, C. et al. (2007) Mol. Psychiatry 12:1129.
6. Sousa, I. et al. (2010) Mol. Autism 1:17.

Bioinformatics

• Uniprot:
  • Q86UE6.2()