Recombinant Human IL-17A (Human Cell-expressed) Protein Summary
| Details of Functionality |
Measured by its ability to induce CXCL1/GRO alpha secretion in HT-29 human colon adenocarcinoma cells. The ED 50 for this effect is 0.12-1.2 ng/mL. Measured by its ability to induce IL-6 secretion by NIH-3T3 mouse embryonic fibroblast cells. Yao, Z. et al. (1995) Immunity 3:811. The ED 50 for this effect is 1.5-7.5 ng/mL. |
| Source |
Human embryonic kidney cell, HEK293-derived human IL-17/IL-17A protein Gly24-Ala155 |
| Accession # |
|
| N-terminal Sequence |
Gly24 |
| Structure / Form |
Disulfide-linked homodimer |
| Protein/Peptide Type |
Recombinant Proteins |
| Gene |
IL17A |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
15.1 kDa (monomer). 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 |
15-23 kDa, reducing conditions 28-38 kDa, non-reducing conditions |
| Publications |
Read Publications using 7955-IL in the following applications:
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Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC 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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 100-500 μg/mL in 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 Human IL-17A (Human Cell-expressed) Protein
Background
Interleukin-17A (IL-17A), also known as CTLA-8, is a 15-20 kDa glycosylated cytokine that plays an important role in anti-microbial and chronic inflammation. The six IL-17 cytokines (IL-17A-F) are encoded by separate genes but adopt a conserved cystine knot fold (1, 2). Mature human IL-17A shares 60% amino acid sequence identity with mouse and rat IL-17A (3, 4). IL-17A is secreted by Th17 cells, gamma /δ T cells, iNKT cells, NK cells, LTi cells, neutrophils, and intestinal Paneth cells (2). It forms disulfide-linked homodimers as well as disulfide-linked heterodimers with IL-17F (5, 6). IL-17A exerts its effects through the transmembrane IL-17 RA in complex with IL-17 RC or IL-17 RD (7, 8). Both IL-17 RA and IL-17 RC are required for responsiveness to heterodimeric IL-17A/F (7). IL-17A promotes protective mucosal and epidermal inflammation in response to microbial infection (9-12). It induces chemokine production, neutrophil influx, and the production of antibacterial peptides (9-11). IL-17A/F likewise induces neutrophil migration, but IL-17F does not (11). IL-17A additionally enhances the production of inflammatory mediators by rheumatoid synovial fibroblasts and contributes to TNF-alpha induced shock (4, 13). In contrast, it can protect against the progression of colitis by limiting chronic inflammation (12). IL-17A encourages the formation of autoreactive germinal centers and exacerbates the onset and progression of experimental models of autoimmunity (14, 15). IL-17A has been shown to exert either tumorigenic or anti-tumor effects (16, 17).
- Gaffen, S.L. (2009) Nat. Rev. Immunol. 9:556.
- Cua, D.J. and C.M. Tato (2010) Nat. Rev. Immunol. 10:479.
- Yao, Z. et al. (1995) J. Immunol. 155:5483.
- Fossiez, F. et al. (1996) J. Exp. Med. 183:2593.
- Chang, S.H. and C. Dong (2007) Cell Res. 17:435.
- Wright, J.F. et al. (2007) J. Biol. Chem. 282:13447.
- Wright, J.F. et al. (2008) J. Immunol. 181:2799.
- Rong, Z. et al. (2009) Cell Res. 19:208.
- Cho, J.S. et al. (2010) J. Clin. Invest. 120:1762.
- Liang, S.C. et al. (2006) J. Exp. Med. 203:2271.
- Liang, S.C. et al. (2007) J. Immunol. 179:7791.
- O’Connor Jr., W. et al. (2009) Nat. Immunol. 10:603.
- Takahashi, N. et al. (2008) J. Exp. Med. 205:1755.
- Hsu, H. et al. (2008) Nat. Immunol. 9:166.
- Rohn, T.A. et al. (2006) Eur. J. Immunol. 36:2857.
- Wang, L. et al. (2009) J. Exp. Med. 206:1457.
- Kryczek, I. et al. (2009) Blood 114:357.
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