Recombinant Mouse FLRT1 His-tag Protein, CF

Recombinant Mouse FLRT1 His-tag Protein (Catalog # 10955-FL) supports the adhesion of Neuro 2A mouse neuroblastoma cells. The ED50 for this effect is 0.500-4.00 µg/mL.

2 μg/lane of Recombinant Mouse FLRT1 His-tag Protein (Catalog # 10955-FL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 65-83 kDa.

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

Recombinant Mouse FLRT1 His-tag Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of Neuro‑2A mouse neuroblastoma cells. The ED₅₀ for this effect is 0.50-4.00 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse FLRT1 protein
  Thr52-Pro552
• Accession #: NP_958813.1
• N-terminal Sequence: Thr52
• 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: 60 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: 65-83 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 Mouse FLRT1 His-tag Protein, CF

• fibronectin leucine rich transmembrane protein 1
• Fibronectin-like domain-containing leucine-rich transmembrane protein 1
• FLRT1
• leucine-rich repeat transmembrane protein FLRT1
• MGC21624
• SPG68

Background

Fibronectin-like domain-containing leucine-rich transmembrane protein 1 (FLRT1) is one of three FLRT leucine-rich repeat transmembrane glycoproteins involved in the regulation of FGF signaling. FLRTs are characterized by an extracellular domain (ECD) with fibronectin and leucine rich repeat (LRR) motifs involved in cell adhesion functions (1). Mature mouse FLRT1 consists of an ECD with 10 N-terminal leucine-rich repeats and a juxtamembrane fibronectin type III domain, a single transmembrane domain and a short cytoplasmic domain lacking defined signaling motifs (1). The ECD of mouse FLRT1 shares 97% amino acid (aa) sequence identity with the ECD of human FLRT1. Both during development and in adulthood, FLRT1 is expressed in distinct areas of the brain and other tissues, including the kidney, and Its expression is distinct from that of FLRT2 and FLRT3 (1, 2). In mouse, FLRT1 is expressed at brain compartmental boundaries in embryos (2). The fibronectin domain of all three FLRTs can bind FGF receptors and this binding is thought to regulate FGF signaling during development (2, 3). The LRR domains are responsible for both the localization of FLRTs in areas of cell contact and homotypic cell-cell association (4). This may be through direct interactions with other FLRT molecules or, as has been shown for FLRT3, by regulating internalization of adhesion molecules such as cadherins (4, 5). Down-regulation of FLRT1 has been associated with prognosis of gastric cancer and has potential to be a therapeutic target for tumor treatment (6).

1. Lacy, S.E. et al. (1999) Genomics 62:417.
2. Haines, B.P. et al. (2006) Dev. Biol. 297:14.
3. Bottcher, R.T. et al. (2004) Nat. Cell Biol. 6:38.
4. Karaulanov, E.E. et al. (2006) EMBO Rep. 7:283.
5. Ogata, S. et al. (2007) Genes Dev. 21:1817.
6. Liang, Y. et al. (2019) Pathol. Res. Pract. 215:152570.

Bioinformatics

• Uniprot:
  • NP_958813.1()