详细说明
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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 Gly24-Ala155
Accession #
N-terminal Sequence
AnalysisGly24
Structure / Form
Disulfide-linked homodimer, Biotinylated via sugars
Predicted Molecular Mass
15 kDa (unlabeled)
SDS-PAGE
14-23 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.
BT7955/CF |
| BT7955 |
Formulation Lyophilized from a 0.2 μm filtered solution in PBS and NaCl. | Formulation Lyophilized from a 0.2 μm filtered solution in PBS and NaCl with BSA as a carrier protein. | |
Reconstitution Reconstitute at 100 μg/mL in PBS. | Reconstitution Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. | |
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | |
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
| Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Data Images
Bioactivity
| Both Biotinylated Recombinant Human IL-17A (Catalog # BT7955/CF) and unlabeled Recombinant Human IL-17A (Catalog # 7955-IL/CF) induces IL-6 secretion by NIH‑3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 1.5-7.5 ng/mL. The similarity in activity highlights that the biotinylated protein is fully functional. |
Background: IL-17/IL-17A
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-17RA in complex with IL-17RC or IL-17RD (7, 8). Both IL-17RA and IL-17RC 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).
References:
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.
Long Name:
Interleukin 17
Entrez Gene IDs:
3605 (Human); 16171 (Mouse); 301289 (Rat); 481837 (Canine)
Alternate Names:
CTLA-8; CTLA8cytotoxic T-lymphocyte-associated serine esterase 8; Cytotoxic T-lymphocyte-associated antigen 8; IL17; IL-17; IL17A; IL-17A; IL-17Acytotoxic T-lymphocyte-associated protein 8; IL-17CTLA-8; IL17interleukin-17A; interleukin 17 (cytotoxic T-lymphocyte-associated serine esterase 8); interleukin 17A