Recombinant Mouse FLRT3 His-tag Protein, CF Summary
Product Specifications
Lys29-Pro528, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
10614-FL
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
![](https://resources.rndsystems.com/images/datasheets/protein/10614-fl_recombinant-mouse-flrt3-his-tag-protein-cf-bioactivity-21122020212533.jpg)
Recombinant Mouse FLRT3 His-tag (Catalog # 10614-FL) supports the adhesion of Neuro 2A mouse neuroblastoma cells. The ED50 for this effect is 0.4-3.6 µg/mL.
![](https://resources.rndsystems.com/images/datasheets/protein/10614-fl_recombinant-mouse-flrt3-his-tag-protein-cf-sds-page-219202014590.jpg)
2 μg/lane of Recombinant Mouse FLRT3 His-tag Protein (Catalog # 10614-FL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 67-87 kDa.
Reconstitution Calculator
Background: FLRT3
Fibronectin-like domain-containing leucine-rich transmembrane protein 3 (FLRT3) is one of three FLRT glycoproteins expressed in distinct areas of the developing brain and other tissues (1, 2). Mouse FLRT3 consists of an extracellular domain (ECD) containing 10 leucine-rich repeats (LRR) and a juxtamembrane fibronectin type III domain, a single transmembrane domain and a cytoplasmic domain (1). The ECD of mature mouse FLRT3 shares 96% amino acid (aa) sequence identity with the ECD of human and rat FLRT3. In mouse embryos, FLRT3 is required to maintain tissue integrity and organize the underlying basement membrane in the anterior visceral endoderm (AVE) (2). The fibronectin domain is responsible for binding to FGF receptors and is thought to regulate FGF signaling during development (3, 4). The LRR domains are responsible for both the localization in areas of cell contact and homotypic cell-cell association (5). This may be through direct interaction with other FLRT molecules, or alternatively, by regulating internalization of adhesion molecules such as cadherins (5, 6). Developmentally, FLRT3 is located in somitic regions on dermatomyotomal muscle precursors and myotomal cells before their migration to the myotome and syndetome, respectively (3). FLRT3 is also expressed at the midbrain/hindbrain boundary and in the apical ectodermal ridge where it may influence FGF signaling (3). Further, FLRT3 is up-regulated and promotes neurite outgrowth following experimental peripheral nerve injury in rats (7, 8). Genetic deletion in mouse embryos results in defective headfold fusion and endoderm migration (9). FLRT3 is a ligand to LPHN1 and maybe involved in the Tim-3-galectin-9 pathway (10). Elevated expression of FLRT3 has been found in breast cancer cells and may serve as a biomarker for head and neck squamous cell carcinoma (HNSCC) (10, 11).
- Lacy, S.E. et al. (1999) Genomics 62:417.
- Egea, et al. (2008) Genes Dev.22:3349.
- Haines, B.P. et al. (2006) Dev. Biol. 297:14.
- Bottcher, R.T. et al. (2004) Nat. Cell Biol. 6:38.
- Karaulanov, E.E. et al. (2006) EMBO Rep. 7:283.
- Ogata, S. et al. (2007) Genes Dev. 21:1817.
- Tsuji, L. et al. (2004) Biochem. Biophys. Res. Commun. 313:1086.
- Robinson, M. et al. (2004) Mol. Cell. Neurosci. 27:202.
- Maretto, S. et al. (2008) Dev. Biol. 318:184.
- Yasinska, I.M. et al. (2019) Front. Immunol. 10:1594.
- Tripathi, N. et al. (2020) J Cell Physiol. 235:9922.
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