Recombinant Mouse FLRT2 His-tag Protein, CF

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Recombinant Mouse FLRT2 His-tag (Catalog # 10715-FL) supports the adhesion of Neuro 2A mouse neuroblastoma cells. The ED50 for this effect is 0.60-4.80 μg/mL.
2 μg/lane of Recombinant Mouse FLRT2 His-tag (Catalog # 10715-FL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 71-80 ...read more

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse FLRT2 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 0.60-4.80 µg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse FLRT2 protein
Cys36-Ser539, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Cys36
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
57 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
71-80 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 FLRT2 His-tag Protein, CF

  • Fibronectin Leucine Rich Transmembrane Protein 2
  • Fibronectin-Like Domain-Containing Leucine-Rich Transmembrane Protein 2
  • FLRT2
  • KIAA0405
  • Leucine-Rich Repeat Transmembrane Protein FLRT2

Background

FLRT2 is one of three FLRT (fibronectin, leucine rich repeat, transmembrane) glycoproteins expressed in distinct areas of the developing brain and other tissues (1, 2). The 85 kDa type I transmembrane (TM) mouse FLRT2 is synthesized as a 660 amino acid (aa) precursor with a 35 aa signal sequence, a 505 aa extracellular domain (ECD), a 21 aa TM segment and a 99 aa cytoplasmic region. The ECD contains 10 N-terminal leucine-rich repeats flanked by cysteine-rich areas, and a juxtamembrane fibronectin type III domain (1). The mouse FLRT2 ECD shares 97% and 99% aa sequence identity with human and rat FLRT2 ECD, respectively. The fibronectin domain of all three FLRTs can bind to FGF receptors (2). 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). In adulthood, FLRT2 mRNA is most abundant in pancreas, but is also present in skeletal muscle, brain and heart (1). FLRT2 in mouse embryos shows highest expression in a subset of the sclerotome in the brain, the stomach, and posterior to the developing heart (2). This expression is distinct from that of FLRT1 and FLRT3 (2). Overexpression of FLRT2 promotes tumor suppression in colorectal and breast cancers (6, 7).
  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. Guo, X. et al. (2020) J. Cancer 11:7329.
  7. Bae, H. et al. (2017) Sci. Rep. 7:272.

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