Recombinant Canine IL-17A Protein

Catalog #: 5848-CL
1 Citation Datasheet / COA / SDS

Carrier Free

Catalog #	Availability	Size / Price	Qty
5848-CL-025/CF

With Carrier

Catalog #	Availability	Size / Price	Qty
5848-CL-025

R&D Systems Recombinant Proteins and Enzymes

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Citations (1)

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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Canine IL-17A Protein Summary

Product Specifications

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain

Endotoxin Level

<0.01 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 ED₅₀ for this effect is 0.3-1.5 ng/mL.

Source

E. coli-derived canine IL-17/IL-17A protein
Gly81-Ala210

Accession #

XP_538958.2

N-terminal Sequence
Analysis

Gly81

Structure / Form

Disulfide-linked homodimer

Predicted Molecular Mass

15.2 kDa (monomer)

SDS-PAGE

14 kDa, reducing conditions

Product Datasheets

5848-CL (with carrier)

Product Datasheet

COA

SDS

5848-CL/CF (carrier free)

Product Datasheet

COA

SDS

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.

5848-CL

Formulation	Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein.
Reconstitution	Reconstitute at 100 μg/mL in 4 mM HCl 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.
Stability & 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.

5848-CL/CF

Formulation	Lyophilized from a 0.2 μm filtered solution in HCl.
Reconstitution	Reconstitute at 100 μg/mL in 4 mM HCl.
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. 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.

Reconstitution Calculator

Background: IL-17/IL-17A

Interleukin 17 (IL-17; also IL-17A and CTLA-8) is a 17 kDa member of the IL-17 family of cytokines (1). 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 (2-4). Based on the amino acid (aa) sequence alignment with human IL-17, canine IL-17 is 130 aa in length. It is secreted as a 35 kDa disulfide-linked homodimer and as a 40 kDa disulfide-linked heterodimer with IL-17F (5). Canine IL-17 is 81% identical on the aa level to human IL-17. IL-23 drives Th17 lymphocytes to produce IL-17 (6-8). IL-17’s production has also been demonstrated in gamma δ T cells (9), CD8⁺ memory T cells (10, 11), eosinophils (12), neutrophils (10), and monocytes (13). Studies have identified that the widely expressed receptors IL‑17RA and IL-17RC form a heterodimer for the binding of IL-17 (6, 14‑15). The predominant function of IL-17 is thought to be as a proinflammatory mediator through a variety of mechanisms (16). Locally, IL-17 stimulates production of IL-6, prostaglandin E and nitric oxide (16-19), and synergy with other inflammatory cytokines such as TNF-alpha, IL-1 beta and IFN -gamma leads to up-regulation of gene expression and progression and amplification of local inflammation (16, 20‑22). IL-17 also mediates chemotaxis of neutrophils and monocytes to sites of inflammation through the chemoattractant mediators IL-8, Gro-alpha, and MCP-1 (16, 22-25) while augmenting production of hematopoietic growth factors, such as G-CSF and GM‑CSF (16, 26, 27), which promote the growth and maturation of the recruited myeloid cells. In addition, IL-17 serves as a bridge between innate and adaptive immune responses by enhancing the induction of co-stimulatory molecules such as ICAM-1 and other cytokines (16, 22, 28), thereby supporting T cell activation. IL-17 expression has been associated with many inflammatory diseases, such as rheumatoid arthritis, multiple sclerosis, asthma, systemic lupus erythematosus and allograft rejection (15).

References

Gaffen, S.L. et al. (2006) Vitam. Horm. 74:255.
Kawaguchi, M. et al. (2004) J. Allergy Clin. Immunol. 114:1265.
Kolls, J.K. and A. Linden (2004) Immunity 21:467.
Moseley, T.A. et al. (2003) Cytokine Growth Factor Rev. 14:155.
Wright, J.F. et al. (2007) J. Biol. Chem. 282:13447.
Cheung, P.F.Y. et al. (2008) J. Immunol. 180:5625.
Steinman, L. (2007) Nat. Med. 13:139.
Hunter, C.A. (2005) Nat. Rev. Immunol. 5:521.
Lockhart, E. et al. (2006) J. Immunol. 177:4662.
Ferretti, S. et al. (2003) J. Immunol. 170:2106.
Shin, H.C. et al. (1999) Cytokine 11:257.
Molet, S. et al. (2001) J. Allergy Clin. Immunol. 108:430.
Zhou, Q. et al. (2005) Infect. Immun. 73:935.
Kuestner, R.E. et al. (2007) J. Immunol. 179:5462.
Chang, S.H. and C. Dong (2007) Cell Res. 17:435.
Afzali, B. et al. (2007) Clin. Exp. Immunol. 148:32.
Fossiez, F. et al. (1996) J. Exp. Med. 183:2593.
Yao, Z. et al. (1995) Immunity 3:811.
Attur, M.G. et al. (1997) Arthritis Rheum. 40:1050.
Ruddy, M.J. et al. (2004) J. Biol. Chem. 279:2559.
Albanesi, C. et al. (1999) J. Immunol. 162:494.
Witowski, J. et al. (2000) J. Immunol. 165:5814.
Miyamoto, M. et al. (2003) J. Immunol. 170:4665.
Ye, P. et al. (2001) Am. J. Respir. Cell Mol. Biol. 25:335.
Laan, M. et al. (2001) Br. J. Pharmacol. 133:200.
Starnes, T. et al. (2002) J. Immunol. 169:642.
Jones, C.E. et al. (2002) Am. J. Respir. Cell Mol. Biol. 26:748.
Yao, Z. et al. (1995) J. Immunol. 155:5483.

Long Name

Interleukin 17

Entrez Gene IDs

3605 (Human); 16171 (Mouse); 301289 (Rat); 449530 (Porcine); 481837 (Canine); 102119976 (Cynomolgus Monkey)

Alternate Names

CTLA8; 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

Related Research Areas

Citation for Recombinant Canine IL-17A Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1