Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs has established a broad range of platforms for developing novel antibodies or equivalents. These cutting-edge technologies enable our scientists to meet your demands from different aspects and tailor the most appropriate solution that contributes to the success of your projects.
HighlightsWith deep understanding in antibody-related realms and extensive project experience, Creative Biolabs offers a variety of references to help you learn more about our capacities and achievements, including infographic, flyer, case study, peer-reviewed publications, and all kinds of knowledge that can assist your projects. You are also welcome to contact us directly for more specific solutions.
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Interleukin-17F (IL-17F) is a potent, disulfide-linked homodimeric cytokine belonging to the IL-17 cytokine family. IL-17F is mainly released by activated T helper 17 (Th17) cells, group 3 innate lymphoid cells (ILC3s), and tissue-resident γδ T cells at mucosal barriers; IL-17F signals through a heteromeric receptor complex composed of IL-17RA and IL-17RC. Although IL-17F was initially viewed as a less prominent paralog of IL-17A, subsequent studies have established it as an important effector cytokine that overlaps with, but is not fully redundant with, IL-17A-mediated responses. Upon receptor binding, IL-17F activates downstream NF-κB and mitogen-activated protein kinase (MAPK) pathways that induce neutrophil-attracting chemokines, epithelial antimicrobial peptides such as β-defensins and S100 proteins, along with pro-inflammatory cytokines that contribute to barrier immune responses; these effects can be further modulated by other inflammatory mediators. Importantly, IL-17F can also form bioactive heterodimers with IL-17A; this configuration displays biological properties that differ from those of either homodimeric cytokine. Aberrantly elevated or prolonged IL-17F signaling has been implicated in inflammatory diseases including plaque psoriasis, psoriatic arthritis, inflammatory bowel disease (IBD), and severe asthma, where sustained cytokine signaling can contribute to epithelial barrier dysfunction and tissue-damaging inflammation. These biological characteristics, together with clinical evidence supporting blockade of the IL-17 signaling pathway, provide a rationale for investigating IL-17F as a target in biologic drug development and as a potential biomarker in precision inflammation research.
Fig.1 IL-17RA/RC signalling pathways.1
IL17F carries out multiple immunological programs that encompass much more than its traditional role as a simplistic pro-inflammatory mediator:
We present a diverse collection of bioactive, correctly folded recombinant IL17F cytokine variants that have been carefully engineered to withstand the unique challenges imposed by immunology research as well as therapeutic antibody screening and high-throughput drug screenings. Knowing that native disulfide-mediated dimerization, accurate N-linked glycosylation, and correct tertiary topology are unambiguous requirements for high-affinity engagement with the IL-17RA/RC receptor complex, our production pipeline focuses on ensuring the correct oligomeric form and structural stability. Our catalog provides high-quality recombinant IL17F homodimers to support diverse experimental needs. All purified preparations are subject to a comprehensive analytical characterization process involving size-exclusion chromatography for oligomeric state assessment, reversed-phase HPLC analysis of purity, intact mass spectrometry (including molecular weight and glycoform profiling), along with appropriate bioactivity validation for research applications.
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The construction of cellular platforms that accurately capture IL17F secretion profiles and receptor-mediated signaling is essential to dissect its function in barrier immunity as well as to facilitate the development of anti-inflammatory therapeutics. Here we describe a stable set of secreted IL17F-expressing cells that utilize lentiviral transduction along with transposon-mediated genomic integration to achieve sustained, physiologically relevant expression levels, authentic secretion kinetics and functional responsiveness following pattern recognition receptor -and cytokine-signalling. We offer not only constitutive wild-type expression, but also tetracycline-inducible systems that allow metastable cytokine "on-demand" release; and co-expression of IL17F as well as its obligate receptor subunits IL-17RA and IL-17RC in a single cellular background. To enable mechanistic interrogation of IL17F-driven inflammation, we further engineered dual-reporter lines that include luciferase cassettes downstream of NF-κB-, AP-1-, or STAT3-response elements to allow for real-time pathway activation quantification after IL17F stimulation or neutralizing antibody blockade. Complementary loss-of-function models—using shRNA-based knockdown or dominant-negative receptor expression--have been developed to perform complementary rescue experiments and synthetic lethality screening. All cell lines are biologically validated by genomic integration mapping, secretion rate profiling using ELISA and functional validation against transwell neutrophil chemotaxis as well as epithelial barrier integrity assays.
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Utilize our carefully crafted portfolio of sequence-defined, high-affinity monoclonal antibodies that have been specifically designed to overcome the structural and immunological biology obstacles associated with this pleotropic cytokine in your IL17F studies. They differentiate with high selectivity the IL17F homodimer from its heterodimeric counterpart (IL17A-IL17F), and they allow for minimal cross-reactivity between IL-17 family paralogs to distinguish non-homologs, and particularly closely-related allelic variants such as human IL-17A; moreover, our antibodies recognize both glycosylated and non-glycosylated isoforms given diverse analytical settings. We have extensively pre-validated these reagents for: sensitive Western blotting under both reducing and non-reducing conditions to assess dimerization and secretion, direct or sandwich ELISA formats in cell culture supernatants and biological fluids, flow cytometric detection of intracellular IL17F following permeabilisation of Th17 and ILC3 populations, high-resolution immunofluorescence-guided confocal microscopy analysis cytokine granules/extracellular deposits (extrusions), formalin-fixed paraffin-embedded psoriatic plaque/colonic tissue sections quantitative analyses by sequentially multi-colour multiplexing as well functional neutralization studies blocking IL17F-dependent NFκB activation/neutrophil chemotaxis.
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In addition to our standard catalog, we also provide fully customized discovery and manufacturing solutions designed for the more advanced-capture requirements of IL17F-targeted therapeutic and diagnostic development:
Yes. Our mammalian expression systems provide single signal peptide cleavage, specific interchain disulfide bridge formation and complete occupancy of N-linked glycosylation sites that define solubility and protease resistance.
Absolutely. Our new monoclonal antibodies are against the unique epitopes in IL17F N-terminal region and helix-loop regions which share little sequence homology with IL-17A, -B, -C, -D or E. The specificity of such antibodies has been confirmed via extensive cross-reactivity testing by Western blot, ELISA, and cell-based neutralization, making them suitable for diagnostic quantification in complex biological matricess.
Certainly. We generate in a facile manner IL17F homodimers, IL17A-IL17F heterodimers and monomeric cysteine-to-serine mutants made to probe dimerization requirements for receptor binding and signaling. These custom-built constructs are provided as purified recombinant proteins) or as genetically stable cell lines, with complete sequence validation followed by mass spectrometric identity confirmation and functional characterization via IL-17RA/RC reporter assays.
Yes. We provide bicistronic and triple-promoter expression systems designed to direct the combined expression of IL17F together with either IL-17RA or IL-17RC into a singular stable cell line. Designed to serve as cellular substrates for immediate utilization in therapeutic screening and mechanistic research, these platforms are functionalally validated for ligand-dependent signaling, antibody neutralization & cross-talk studies of cytokines.
