• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.01 EU per 1 μg of the protein by the LAL method.  

• Activity

  Bioassay data are not available.

• Source

  Mouse myeloma cell line, NS0-derived Ala27-Arg299, with a C-terminal 6-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Ala27

• Predicted Molecular Mass

  32 kDa

• SDS-PAGE

  55-63 kDa, reducing conditions

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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: IL-17 RD/SEF

Interleukin-17 receptor D (IL-17 RD), also known as SEF (similar expression to FGFs), is a type I transmembrane protein that is found in both the cytoplasm and plasma membrane (1 - 5). The gene for this protein belongs to a synexpression group originally identified in zebrafish where SEF is expressed along with FGF-3, -8, sprouty-2 (SPRY2) and SPRY4 (6, 7). By alternate splicing, two transcript variants, potentially encoding three protein isoforms, exist. One is a full-length long form, one a shortened form that uses an alternate start site, and one an alternate splice form that removes the classic signal sequence (1 - 4). These isoforms have different expression patterns, subcellular localization, and function. The membrane-bound long form of human IL-17RD is synthesized as a 739 amino acid (aa) precursor protein with a putative 27 aa signal peptide, a 272 aa extracellular domain, a 20 aa transmembrane segment and a 420 aa cytoplastic domain. The extracellular domain contains one Ig-like domain and a fibronectin type III motif. The cytoplasmic domain shares homology with the intracellular domains of IL-17 receptor family members and shows one TIR (Toll/IL-1 Receptor) domain and a putative TRAF6-binding motif (2). Natural IL-17 RD has been shown to form homomultimeric complexes (3). Unlike the alternate splice form of IL-17 RD that has a restricted pattern of expression, the full-length IL-17 RD isoform is expressed in most adult tissues and during embryonic development (3, 5). Functionally, IL-17 RD has been shown to be an inhibitor of FGF signaling. The molecule’s extracellular domain does not seem to be involved. There is an interaction between the intracellular domains of FGFR1/2 and IL-17 RD that blocks ERK dissociation from MEK, thereby interfering with downstream ERK activation of nuclear Elk-1 (8). IL-17 RD has also been reported to interact with TAK1 and induce JNK activation and apoptosis (9). Ligands that interact with the extracellular domain of IL-17 RD have not been identified.

• References:

1. Furthauer, M. et al. (2002) Nat. Cell Biol. 4:170.

2. Xiong, S. et al. (2003) J. Biol. Chem. 278:50273.

3. Yang, R.-B. et al. (2003) J. Biol. Chem. 278:33232.

4. Preger, E. et al. (2003) Proc. Natl. Acad. Sci. USA 101:1229.

5. Lin, W. et al. (2002) Mech. Dev. 113:163.

6. Tsang, M. et al. (2002) Nat. Cell Biol. 4:165.

7. Kovalenko, D. et al. (2003) J. Biol. Chem. 278:14087.

8. Torii, S. et al. (2004) Dev. Cell 7:33.

9. Yang, X. et al. (2004) J. Biol. Chem. 279:38099.

• Long Name:

  Interleukin 17 Receptor D, Transcript Variant 3

• Entrez Gene IDs:

  54756 (Human); 171463 (Mouse)

• Alternate Names:

  FLJ35755; IL-17 RD; IL17RD; IL-17RD; IL-17RDIL-17 receptor D; IL17Rhom; IL17RLM; IL17RLMDKFZp434N1928; interleukin 17 receptor D; interleukin-17 receptor D; Interleukin-17 receptor-like protein; MGC133309; Sef homolog; SEF; SEFhSef