Recombinant Mouse IL-17RD/SEF Protein

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity

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Recombinant Mouse IL-17RD/SEF Protein Summary

Details of Functionality
Bioassay data are not available.
Source
Mouse myeloma cell line, NS0-derived mouse IL-17 RD/SEF protein
Gly28-Arg299, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Gly28
Structure / Form
Monomer
Protein/Peptide Type
Recombinant Proteins
Gene
Il17rd
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
31.6 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
54-60 kDa, 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 with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse IL-17RD/SEF Protein

  • 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

Background

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 and SEF is expressed along with FGF-3, -8, sprouty-2 (SPRY2) and SPRY4 (6, 7). Due to the presence of an alternate start site, there is one transcript that potentially gives rise to two isoforms. The first is a full-length long form and the second an N-terminally truncated form (2, 5). The significance and expression pattern of the short form are uncertain. The membrane-bound long form of mouse IL-17 RD is synthesized as a 738 amino acid (aa) precursor protein with a putative 27 aa signal peptide, a 272 aa extracellular domain, a 20 aa transmembrane segment and a 419 aa cytoplastic domain (5). 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). 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.

  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.

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Bioinformatics

Gene Symbol Il17rd
Uniprot