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Recombinant Cynomolgus/Rhesus Macaque IL-17F His Protein, CF

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Recombinant Cynomolgus Monkey/Rhesus Macaque IL-17F (Catalog # 10225-IL) induces IL-6 secretion by NIH-3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 5-40 ng/mL.
2 μg/lane of Recombinant Cynomolgus/Rhesus Macaque IL-17F His-tag (Catalog # 10225-IL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity Pm-Cm, RMSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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Recombinant Cynomolgus/Rhesus Macaque IL-17F His Protein, CF Summary

Details of Functionality
Measured by its ability to induce IL-6 secretion by NIH‑3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 5-40 ng/mL
Source
Chinese Hamster Ovary cell line, CHO-derived IL-17F protein
Arg31-Gln163, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Arg31
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, 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
16 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
17-25 kDa, under 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.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Cynomolgus/Rhesus Macaque IL-17F His Protein, CF

  • Cytokine ML-1
  • IL17F
  • IL-17F
  • IL-17Finterleukin-17F
  • interleukin 17F

Background

The Interleukin 17 (IL-17) protein family, composed of six members (IL-17A through IL-17F), are secreted, structurally related proteins that share a conserved cystine-knot fold near the C-terminus, but have considerable sequence divergence at the N‑terminus. With the exception of IL-17B which exists as a non-covalently linked dimer, all IL-17 family members are disulfide-linked dimers. IL-17 proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions (1, 2). Cynomolgus IL-17F cDNA encodes a 163 amino acid (aa) protein with a putative 30 aa signal peptide. Mature cynomolgus IL-17F shares 96% and 100% aa sequence identity with human and rhesus macaque IL-17F, respectively. IL-17F is expressed in activated CD4+ T-cells and activated monocytes. Five receptors (IL-17 RA-RE) have been identified. Although the ligands for IL-17 RD and RE are not known yet, it is reported that IL-17 RA binds IL-17A, and IL-17 RB binds IL-17B and IL-17E. IL-17 RC binds IL‑17A and IL‑17F with similarly high affinity and functions as a receptor for both IL-17A and IL‑17F (3, 4). The biological activities mediated by IL-17F are similar to those of IL-17A. IL-17F stimulates production of IL-6, IL-8, G-CSF, and regulates cartilage matrix turnover by increasing matrix release and inhibiting new matrix synthesis (5). IL-17F also inhibits angiogenesis and induces production of IL-2, TGF-beta, and monocyte chemoattractant protein-1 in endothelial cells (6).
  1. Aggarwal, S. and A.L. Gurney (2002) J. Leukoc. Biol. 71:1.
  2. Moseley, T.A. et al. (2003) Cytokine & Growth Factor Rev. 14:155.
  3. Kuestner, R.E. et al. (2007) J. Immunol. 179:5462.
  4. Shen, F. & S. L. Gaffen (2008) Cytokine 41:92.
  5. Hot, A. and Miossec, P. (2011) Ann. Rheum. Dis. 70:727.
  6. Starnes, T. et al. (2001) J. Immunol. 167:4137.

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