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.
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
>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
Publications
Read Publication using 9640-IL in the following applications:
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).
Pappu, R. et al. (2012) Trends Immunol. 33:343.
Rubino, S.J. et al. (2012) Trends Immunol. 33:112.
Li, H. et al. (2000) Proc. Natl. Acad. Sci. USA 97:773.
Ramirez-Carrozzi, V. et al. (2011) Nat. Immunol. 12:1159.
Chang, S.H. et al. (2011) Immunity 35:611.
Song, X. et al. (2011) Nat. Immunol. 12:1151.
Pfeifer, P. et al. (2012) Am. J. Respir. Cell Mol. Biol. 48:415.
Johnston, A. et al. (2013) J. Immunol. 190:2252.
Yamaguchi, Y. et al. (2007) J. Immunol. 179:7128.
Johansen, C. et al. (2009) Br. J. Dermatol. 160:319.
Reynolds, J.M. et al. (2012) J. Immunol. 189:4226.
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