Recombinant Human FLRT2 Protein, CF

Recombinant Human FLRT2 Protein, CF Summary

• R&D Systems NS0-derived Recombinant Human FLRT2 Protein (2877-FL)
• Quality control testing to verify active proteins with lot specific assays by in-house scientists
• All R&D Systems proteins are covered with a 100% guarantee

Product Specifications

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.

Background: FLRT2

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) human FLRT2 is synthesized as a 660 amino acid (aa) precursor with a 35 aa signal sequence, a 506 aa extracellular domain (ECD), a 21 aa TM segment and a 98 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 human FLRT2 ECD shares 97%, 96%, 99%, 96% and 95% aa sequence identity with mouse, rat, equine, canine and bovine FLRT2 ECD, respectively. Human FLRT1 and FLRT3 ECDs share approximately 47% aa identity with FLRT2. 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).

Related Research Areas

• Extracellular Matrix and Related Molecules
• Extracellular Matrix Molecules
• FGF Family