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Recombinant Human IL-17C (CHO-expressed) Protein

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When Recombinant Human IL‑17 RE Chimera (Catalog # 8358‑MR) is immobilize at 0.06 μg/mL, Recombinant Human IL‑17C (Catalog # 9640-IL) bindswith an ED50 of 0.2‑1.2 ng/mL.

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human IL-17C (CHO-expressed) Protein Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human IL‑17 RE Fc Chimera (Catalog # 8358-MR) is immobilize at 0.06 μg/mL, 100 μL/well, it binds Recombinant Human IL‑17C. The concentration of Recombinant Human IL‑17C that produces 50% of the optimal binding response is 0.2‑1.2 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human IL-17C protein
His19-Val197
Accession #
N-terminal Sequence
His19
Protein/Peptide Type
Recombinant Proteins
Purity
>90%, 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
20 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
19-25 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 with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 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-17C (CHO-expressed) Protein

  • CX2
  • Cytokine CX2
  • IL17C
  • IL-17C
  • IL-17CMGC126884
  • interleukin 17C
  • interleukin-17C
  • MGC138401

Background

Interleukin-17C (IL-17C) is a 15-20 kDa glycosylated cytokine that plays an important role in mucosal immunity 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-17C shares 79% and 76% amino acid sequence identity with mouse and rat IL-17C, respectively (3). IL-17C binds to IL-17 RE with high affinity and to IL-17 RA with low affinity (4, 5). These two receptor chains can associate into a heterodimeric receptor for IL-17C (4-6). IL-17 RE is expressed on keratinocytes, mucosal epithelial cells, Th17 cells, and g/d T cells, while IL-17 RA is widely expressed (4, 5). IL-17 RE is required for mediating the pro-inflammatory and homeostatic actions of IL-17C in the skin and mucosa (1, 2). IL-17C expression is induced by inflammatory stimulation in colon and airway epithelial cells, keratinocytes, CD4+ T cells, macrophages, and dendritic cells (4, 6-9). It is up-regulated in various chronic inflammatory diseases including psoriasis, cystic fibrosis, and chronic obstructive pulmonary disease (COPD) (7, 8, 10). IL-17 RE is reciprocally down-regulated in psoriatic lesions (10). The interaction of IL-17C with IL-17 RE promotes mucosal immunity through the induction of anti-bacterial peptides and pro‑inflammatory cytokines and chemokines (4, 6, 8, 9). IL-17C action supports the integrity of the colon epithelium following infection induced damage (4, 6, 11) but also contributes to psoriatic skin thickening and the progression of arthritis (4, 8, 9). IL-17C is additionally upregulated in Th17 cell dependent autoimmunity (5). In this setting, it exacerbates disease severity by inducing Th17 cell production of IL-17A, IL-17F, IL-22, CCR6, and CCL20 (5).
  1. Pappu, R. et al. (2012) Trends Immunol. 33:343.
  2. Rubino, S.J. et al. (2012) Trends Immunol. 33:112.
  3. Li, H. et al. (2000) Proc. Natl. Acad. Sci. USA 97:773.
  4. Ramirez-Carrozzi, V. et al. (2011) Nat. Immunol. 12:1159.
  5. Chang, S.H. et al. (2011) Immunity 35:611.
  6. Song, X. et al. (2011) Nat. Immunol. 12:1151.
  7. Pfeifer, P. et al. (2012) Am. J. Respir. Cell Mol. Biol. 48:415.
  8. Johnston, A. et al. (2013) J. Immunol. 190:2252.
  9. Yamaguchi, Y. et al. (2007) J. Immunol. 179:7128.
  10. Johansen, C. et al. (2009) Br. J. Dermatol. 160:319.
  11. Reynolds, J.M. et al. (2012) J. Immunol. 189:4226.

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