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Recombinant Mouse SLITRK1 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse SLITRK1 Protein, CF Summary

Details of Functionality
Measured by its ability to enhance neurite outgrowth of dissociated E13 chick embryonic dorsal root ganglia (DRG) neurons. Able to significantly enhance neurite outgrowth when immobilized as a 3 µL droplet containing 25 ng on a nitrocellulose-coated microplate.
Source
Mouse myeloma cell line, NS0-derived mouse SLITRK1 protein
Asn18-Ser616, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Asn18
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
68 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
84-108 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 Mouse SLITRK1 Protein, CF

  • FLJ54428
  • KIAA1910KIAA0918
  • leucine rich repeat containing 12
  • Leucine-rich repeat-containing protein 12
  • LRRC12
  • RP11-395N17.1
  • SLIT and NTRK-like family, member 1
  • SLIT and NTRK-like protein 1
  • slit and trk like gene 1
  • SLITRK1
  • TTM

Background

SLITRK1 (Slit and Trk-like family member 1) is a charter member of the SLITRK family of proteins (1, 2). This family currently includes six members, all of which contain a slit-like extracellular region and a Trk-like cytoplasmic region except SLITRK1 (3). Mouse SLITRK1 is a type I transmembrane protein of 696 amino acids (aa). It contains a 17 aa signal sequence, a 605 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 53 aa cytoplasmic region. The ECD is characterized by the presence of two leucine-rich domains (LRD) that resemble those found in Slit. Each LRD contains six leucine-rich repeats (LRRs), followed by a Cys-rich, C-terminal LRR. The exact function of the LRRs is not known. Based on other LRRs, it might be assumed that they mediate protein-protein-interaction (4). There are multiple, single aa mutations in the ECD, their significance is unclear (5). One truncating frameshift mutation (a unique 27 aa substitution after Arg421) is associated with Tourette's Syndrome (6). As noted, the cytoplasmic region of SLITRK1 is unique among SLITRK family members. It contains no known signaling motifs, which is in contrast to SLITRK2-6 which show TrkA-like tyrosine phosphorylation sites. This difference is reflected in their function. SLITRK1 is a protein that is found in adult neurons of the cerebrum, thalamus and hippocampus. It induces neurite outgrowth whereas SLITRK2-6 block neurite extension (3) and bind and form complexes with LAR-RPTP's at functional synapses (7). Mouse SLITRK1 shares 98% and 94% aa sequence identity with human and rat SLITRK1, respectively.
  1. Aruga, J. et al. (2003) Gene 315:87.
  2. Nagase, T. et al. (2001) DNA Res. 8:179.
  3. Aruga, J. & K. Mikoshiba, (2003) Mol. Cell. Neurosci. 24:117.
  4. Enkhbayar, P. et al. (2003) Proteins 54:394.
  5. Zuchner, S. et al. (2006) Mol. Psychiat. 11:888.
  6. Abelson, J.F. et al. (2005) Science 310:317.
  7. Um, J.W. et al. (2014) Nat. Commun. 5:5423.

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