Recombinant Human IL-17RC Isoform 1 Fc Chimera Protein, CF

When Recombinant HumanIL-17 RC Isoform 1 Fc Chimera (Catalog #9284-IL) is coated at 0.5 µg/mL, Recombinant Human IL-17/IL-17A (Catalog # 7955-IL) binds with an ED50 = 0.1-0.6 ng/mL.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IL-17RC Isoform 1 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human IL-17RC Isoform 1 Fc Chimera (Catalog # 9284-IL) is coated at 0.5 µg/mL, Recombinant Human IL-17/IL-17A (Catalog # 7955-IL) binds with an ED₅₀ = 0.1-0.6 ng/mL.
• Source: Human embryonic kidney cell, HEK293-derived human IL-17 RC protein
  

  Human IL-17 RC Isoform 1 (Leu21-His465) Accession # NP_703190.1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: NP_703190.1
• N-terminal Sequence: Leu21
• Structure / Form: Disulfide-linked homodimer
• 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: 76 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: 95-113 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.
• 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 Human IL-17RC Isoform 1 Fc Chimera Protein, CF

• FLJ95963
• FLJ96005
• IL-17 RC
• IL-17 receptor C
• IL-17 RL
• IL17F receptor
• IL17RC
• IL-17RC
• IL17Rhom
• IL17RL
• IL-17RL
• IL17-RL
• interleukin 17 receptor C
• interleukin-17 receptor C
• Interleukin-17 receptor homolog
• Interleukin-17 receptor-like protein
• MGC10763
• zcytoR14

Background

IL-17 receptor C (IL-17RC; also known as IL-17RL and IL-17Rhom) is an 85-110 kDa member of the IL-17 receptor family. IL-17 plays a key role in the development of autoimmunity and inflammation (1, 2). Human IL-17 RC is a type I transmembrane glycoprotein that is expressed on neutrophils, endothelial cells, chondrocytes and osteoblasts, breast and prostatic epithelium, fibroblasts, renal tubular epithelium, and skeletal muscle cells (3-5). Mature human IL-17 RC consists of a 518 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 232 aa cytoplasmic region (6). It is estimated that there are over 90 alternative splice forms, with transmembrane-containing isoforms predominating (4, 7). This recombinant protein corresponds to IL-17 RC isoform 1, the canonical form. Within the ECD, IL-17 RC isoform 1 shares 69% aa sequence identity with mouse IL-17 RC. IL-17 RC is the cognate receptor for IL-17F, and it binds IL-17A with similar affinity (8). IL-17 RC associates wiith IL-17 RA to form a receptor complex for both IL-17A and IL-17F (8-11).

1. Song, X. and Y. Qian (2013) Cytokine 62:175.
2. Weaver, C.T. et al. (2007) Annu. Rev. Immunol. 25:821.
3. Taylor, P.R. et al. (2014) Nat. Immunol. 15:143.
4. You, Z. et al. (2007) Neoplasia 9:464.
5. Kokubu, T. et al. (2008) J. Hictochem. Cytochem. 56:89.
6. Haudenschild, D. et al. (2002) J. Biol. Chem. 277:4309.
7. Haudenschild, D.R. et al. (2006) Prostate 66:1268.
8. Kuestner, R.E. et al. (2007) J. Immunol. 179:5462.
9. Toy, D. et al. (2006) J. Immunol. 177:36.
10. Kramer, J.M. et al. (2006) J. Immunol. 176:711.
11. Kramer, J.M. et al. (2007) J. Immunol. 179:6379.

Bioinformatics

• Uniprot:
  • NP_703190.1()