Recombinant Human IL-17A/F Heterodimer Biotin Protein, CF

Both Biotinylated Recombinant Human IL-17A/F (Catalog # BT5837/CF) and unlabeled Recombinant Human IL‑17A/F Heterodimer (Catalog # 5837-IL) induces IL-6 secretion by NIH‑3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 0.4-2 ng/mL. The similarity in activity highlights that the biotinylated protein is fully functional.

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

Recombinant Human IL-17A/F Heterodimer Biotin Protein, CF Summary

• Details of Functionality: Measured by its ability to induce IL-6 secretion by NIH‑3T3 mouse embryonic fibroblast cells. The ED₅₀ for this effect is 0.4‑2 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human IL-17A/F Heterodimer protein
  

  Human IL-17A (Gly24-Ala155) Accession # Q16552

  Human IL-17F (Arg21-GLN163) Accession # Q96PD4
  N-terminus	C-terminus

• N-terminal Sequence: Gly24(IL-17A) & Arg21(IL-17F)
• Structure / Form: Disulfide-linked heterodimer, Biotinylated via sugars
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 15 kDa (unlabeled IL-17A), 15 kDa (unlabeled IL-17F).
  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.

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 HCl with Trehalose.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in 4 mM HCl.

Notes

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

Alternate Names for Recombinant Human IL-17A/F Heterodimer Biotin Protein, CF

• CTLA8
• CTLA8cytotoxic T-lymphocyte-associated serine esterase 8
• Cytotoxic T-lymphocyte-associated antigen 8
• Cytotoxic T-Lymphocyte-Associated Protein 8
• IL17
• IL-17
• IL-17A
• IL-17A/F Heterodimer
• interleukin 17 (cytotoxic T-lymphocyte-associated serine esterase 8)
• interleukin 17A
• interleukin-17A

Background

Human IL-17A/F is an approximately 40 kDa, secreted, disulfide-linked heterodimeric glycoprotein comprised of two members of the IL-17 family of cytokines, IL-17A and IL-17F (1, 2). Members of this family demonstrate a structural motif termed a cysteine knot that also characterizes a large superfamily of growth factors. Although most cysteine knot superfamily members use three intrachain disulfide bonds to create a knot, IL-17 family molecules generate the same structural form with only two disulfide links (3-5). Mature human IL-17A and IL-17F share 61% and 56% amino acid sequence identity with mouse IL-17A and IL-17F, respectively. They share 50% aa sequence identity with each other. IL-17A/F and the IL-17A and IL-17F homodimers are produced by IL-23 activated Th17 cells (1, 6-10). The widely expressed receptors IL-17 RA and IL-17 RC form a heterodimer for the binding of IL-17A and IL-17F, as well as the heterodimeric IL-17A/F (6, 11, 12). IL-17A/F is a biologically active protein that induces chemokine production and airway neutrophilia with intermediate potency between IL-17A (most potent) and IL-17F (least potent) (7, 12). It is up-regulated in immune cells during inflammatory arthritis and contributes to disease severity (13).

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2. Chang, S.H. and C. Dong (2007) Cell Res. 17:435.
3. Kawaguchi, M. et al. (2004) J. Allergy Clin. Immunol. 114:1265.
4. Kolls, J.K. and A. Linden (2004) Immunity 21:467.
5. Gu, C. et al. (2013) Cytokine 64:477.
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7. Liang, S.C. et al. (2007) J. Immunol. 179:7791.
8. Ouyang, W. et al. (2008) Immunity 28:454.
9. Steinman, L. (2007) Nat. Med. 13:139.
10. Hunter, C.A. (2005) Nat. Rev. Immunol. 5:521.
11. Kuestner, R.E. et al. (2007) J. Immunol. 179:5462.
12. Wright, J.F. et al. (2008) J. Immunol. 181:2799.
13. Sarkar, S. et al. (2014) Clin. Exp. Immunol. 177:652.