Human IL-17F Alexa Fluor® 350-conjugated Antibody
Human IL-17F Alexa Fluor® 350-conjugated Antibody Summary
Gly21-Thr153
Accession # Q96PD4
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
Background: IL-17F
The Interleukin 17 (IL-17) family proteins, comprising 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 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions (1, 2).
Human IL‑17F cDNA encodes a 163 amino acid (a) protein with a putative 30 aa signal peptide. Among IL‑17 family members, IL‑17F is most closely related to IL‑17A (approximately 44% aa sequence homology), but shares only limited sequence homology (16‑30%) with IL-17B, C, D and E. Human and mouse IL-17F share 55% sequence identity. IL-17F is expressed in activated CD4+ T-cells and activated monocytes. Five receptors (IL-17 RA, B, C, D and E) have been identified (5). Although the ligands for IL-17 RD and E 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 (5, 6). The biological activities mediated by IL‑17F are similar to those of
IL‑17. 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 (4).
IL‑17F also inhibits angiogenesis and induces production of IL‑2, TGF-beta, and monocyte chemoattractant protein‑1 in endothelial cells (3).
Product Datasheets
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