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il 17c  (R&D Systems)


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    Structured Review

    R&D Systems il 17c
    Il 17c, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+il+17c/Recombinant+Human+IL-17C+Protein/10__64943_slash_ljmas__2026__04133-89-22-23
    Average 94 stars, based on 11 article reviews
    il 17c - by Bioz Stars, 2026-09
    94/100 stars

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    Related Articles

    Binding Assay:

    Article Title: Specific and high affinity binding proteins comprising modified SH3 domains of FYN kinase
    Article Snippet: A small signal above background was observed for IL-17F, but when 2C1 was probed to a IL-17F coated BIAcore chip, no detectable binding was determined (data not shown). .. Methods a) Specificity For the determination of the binding specificity of IL-17A-binding polypeptides of the invention, the following target proteins were used (more target proteins compared to Example 2.6): human IL-17A (R & D Systems) human IL-17B (Peprotech) human IL-17C (R & D Systems) human IL-17D (Peprotech) human IL-17E (Peprotech) human IL-17F (Abd Serotec) mouse IL-17A (R & D Systems) rat IL-17A (Akron Biotech) canine IL-17A (R & D Systems) cynomolgus (macaca fascicularis) IL-17A (produced in-house in E. coli, without signal peptide, with a C-terminal glycine residue followed by a hexa-his tag, refolded from inclusion bodies, SEQ ID NO: 132) extra domain B of fibronectin (produced in-house, E. coli; see Carnemolla et al. (1996) Int J Cancer, 68(3), p. 397-405) Human IL-6 (R & D Systems) Human TNF alpha (Thermo Scientific) Ovalbumin (Sigma) BSA (Sigma) The target proteins were coated on a MaxiSorp plate (Nunc) overnight (100 μl of each target at a concentration of 10 μg/ml). ..

    Article Title: Specific and high affinity binding proteins comprising modified SH3 domains of FYN kinase
    Article Snippet: A small signal above background was observed for IL-17F, but when 2C1 was probed to a IL-17F coated BIAcore chip, no detectable binding was determined (data not shown). .. Methods a) Specificity For the determination of the binding specificity of IL-17A-binding polypeptides of the invention, the following target proteins were used (more target proteins compared to Example 2.6): human IL-17A (R & D Systems) human IL-17B (Peprotech) human IL-17C (R & D Systems) human IL-17D (Peprotech) human IL-17E (Peprotech) human IL-17F (Abd Serotec) mouse IL-17A (R & D Systems) rat IL-17A (Akron Biotech) canine IL-17A (R & D Systems) cynomolgus (Macaca fascicularis) IL-17A (produced in-house in E. coli, without signal peptide, with a C-terminal glycine residue followed by a hexa-his tag, refolded from inclusion bodies, SEQ ID NO: 132) extra domain B of fibronectin (produced in-house, E. coli; see Carnemolla et al. (1996) Int J Cancer, 68(3), p. 397-405) Human IL-6 (R & D Systems) Human TNF alpha (Thermo Scientific) Ovalbumin (Sigma) BSA (Sigma) The target proteins were coated on a MaxiSorp plate (Nunc) overnight (100 μl of each target at a concentration of 10 μg/ml). ..

    Produced:

    Article Title: Specific and high affinity binding proteins comprising modified SH3 domains of FYN kinase
    Article Snippet: A small signal above background was observed for IL-17F, but when 2C1 was probed to a IL-17F coated BIAcore chip, no detectable binding was determined (data not shown). .. Methods a) Specificity For the determination of the binding specificity of IL-17A-binding polypeptides of the invention, the following target proteins were used (more target proteins compared to Example 2.6): human IL-17A (R & D Systems) human IL-17B (Peprotech) human IL-17C (R & D Systems) human IL-17D (Peprotech) human IL-17E (Peprotech) human IL-17F (Abd Serotec) mouse IL-17A (R & D Systems) rat IL-17A (Akron Biotech) canine IL-17A (R & D Systems) cynomolgus (macaca fascicularis) IL-17A (produced in-house in E. coli, without signal peptide, with a C-terminal glycine residue followed by a hexa-his tag, refolded from inclusion bodies, SEQ ID NO: 132) extra domain B of fibronectin (produced in-house, E. coli; see Carnemolla et al. (1996) Int J Cancer, 68(3), p. 397-405) Human IL-6 (R & D Systems) Human TNF alpha (Thermo Scientific) Ovalbumin (Sigma) BSA (Sigma) The target proteins were coated on a MaxiSorp plate (Nunc) overnight (100 μl of each target at a concentration of 10 μg/ml). ..

    Article Title: Specific and high affinity binding proteins comprising modified SH3 domains of FYN kinase
    Article Snippet: A small signal above background was observed for IL-17F, but when 2C1 was probed to a IL-17F coated BIAcore chip, no detectable binding was determined (data not shown). .. Methods a) Specificity For the determination of the binding specificity of IL-17A-binding polypeptides of the invention, the following target proteins were used (more target proteins compared to Example 2.6): human IL-17A (R & D Systems) human IL-17B (Peprotech) human IL-17C (R & D Systems) human IL-17D (Peprotech) human IL-17E (Peprotech) human IL-17F (Abd Serotec) mouse IL-17A (R & D Systems) rat IL-17A (Akron Biotech) canine IL-17A (R & D Systems) cynomolgus (Macaca fascicularis) IL-17A (produced in-house in E. coli, without signal peptide, with a C-terminal glycine residue followed by a hexa-his tag, refolded from inclusion bodies, SEQ ID NO: 132) extra domain B of fibronectin (produced in-house, E. coli; see Carnemolla et al. (1996) Int J Cancer, 68(3), p. 397-405) Human IL-6 (R & D Systems) Human TNF alpha (Thermo Scientific) Ovalbumin (Sigma) BSA (Sigma) The target proteins were coated on a MaxiSorp plate (Nunc) overnight (100 μl of each target at a concentration of 10 μg/ml). ..

    Residue:

    Article Title: Specific and high affinity binding proteins comprising modified SH3 domains of FYN kinase
    Article Snippet: A small signal above background was observed for IL-17F, but when 2C1 was probed to a IL-17F coated BIAcore chip, no detectable binding was determined (data not shown). .. Methods a) Specificity For the determination of the binding specificity of IL-17A-binding polypeptides of the invention, the following target proteins were used (more target proteins compared to Example 2.6): human IL-17A (R & D Systems) human IL-17B (Peprotech) human IL-17C (R & D Systems) human IL-17D (Peprotech) human IL-17E (Peprotech) human IL-17F (Abd Serotec) mouse IL-17A (R & D Systems) rat IL-17A (Akron Biotech) canine IL-17A (R & D Systems) cynomolgus (macaca fascicularis) IL-17A (produced in-house in E. coli, without signal peptide, with a C-terminal glycine residue followed by a hexa-his tag, refolded from inclusion bodies, SEQ ID NO: 132) extra domain B of fibronectin (produced in-house, E. coli; see Carnemolla et al. (1996) Int J Cancer, 68(3), p. 397-405) Human IL-6 (R & D Systems) Human TNF alpha (Thermo Scientific) Ovalbumin (Sigma) BSA (Sigma) The target proteins were coated on a MaxiSorp plate (Nunc) overnight (100 μl of each target at a concentration of 10 μg/ml). ..

    Article Title: Specific and high affinity binding proteins comprising modified SH3 domains of FYN kinase
    Article Snippet: A small signal above background was observed for IL-17F, but when 2C1 was probed to a IL-17F coated BIAcore chip, no detectable binding was determined (data not shown). .. Methods a) Specificity For the determination of the binding specificity of IL-17A-binding polypeptides of the invention, the following target proteins were used (more target proteins compared to Example 2.6): human IL-17A (R & D Systems) human IL-17B (Peprotech) human IL-17C (R & D Systems) human IL-17D (Peprotech) human IL-17E (Peprotech) human IL-17F (Abd Serotec) mouse IL-17A (R & D Systems) rat IL-17A (Akron Biotech) canine IL-17A (R & D Systems) cynomolgus (Macaca fascicularis) IL-17A (produced in-house in E. coli, without signal peptide, with a C-terminal glycine residue followed by a hexa-his tag, refolded from inclusion bodies, SEQ ID NO: 132) extra domain B of fibronectin (produced in-house, E. coli; see Carnemolla et al. (1996) Int J Cancer, 68(3), p. 397-405) Human IL-6 (R & D Systems) Human TNF alpha (Thermo Scientific) Ovalbumin (Sigma) BSA (Sigma) The target proteins were coated on a MaxiSorp plate (Nunc) overnight (100 μl of each target at a concentration of 10 μg/ml). ..

    Concentration Assay:

    Article Title: Specific and high affinity binding proteins comprising modified SH3 domains of FYN kinase
    Article Snippet: A small signal above background was observed for IL-17F, but when 2C1 was probed to a IL-17F coated BIAcore chip, no detectable binding was determined (data not shown). .. Methods a) Specificity For the determination of the binding specificity of IL-17A-binding polypeptides of the invention, the following target proteins were used (more target proteins compared to Example 2.6): human IL-17A (R & D Systems) human IL-17B (Peprotech) human IL-17C (R & D Systems) human IL-17D (Peprotech) human IL-17E (Peprotech) human IL-17F (Abd Serotec) mouse IL-17A (R & D Systems) rat IL-17A (Akron Biotech) canine IL-17A (R & D Systems) cynomolgus (macaca fascicularis) IL-17A (produced in-house in E. coli, without signal peptide, with a C-terminal glycine residue followed by a hexa-his tag, refolded from inclusion bodies, SEQ ID NO: 132) extra domain B of fibronectin (produced in-house, E. coli; see Carnemolla et al. (1996) Int J Cancer, 68(3), p. 397-405) Human IL-6 (R & D Systems) Human TNF alpha (Thermo Scientific) Ovalbumin (Sigma) BSA (Sigma) The target proteins were coated on a MaxiSorp plate (Nunc) overnight (100 μl of each target at a concentration of 10 μg/ml). ..

    Article Title: Specific and high affinity binding proteins comprising modified SH3 domains of FYN kinase
    Article Snippet: A small signal above background was observed for IL-17F, but when 2C1 was probed to a IL-17F coated BIAcore chip, no detectable binding was determined (data not shown). .. Methods a) Specificity For the determination of the binding specificity of IL-17A-binding polypeptides of the invention, the following target proteins were used (more target proteins compared to Example 2.6): human IL-17A (R & D Systems) human IL-17B (Peprotech) human IL-17C (R & D Systems) human IL-17D (Peprotech) human IL-17E (Peprotech) human IL-17F (Abd Serotec) mouse IL-17A (R & D Systems) rat IL-17A (Akron Biotech) canine IL-17A (R & D Systems) cynomolgus (Macaca fascicularis) IL-17A (produced in-house in E. coli, without signal peptide, with a C-terminal glycine residue followed by a hexa-his tag, refolded from inclusion bodies, SEQ ID NO: 132) extra domain B of fibronectin (produced in-house, E. coli; see Carnemolla et al. (1996) Int J Cancer, 68(3), p. 397-405) Human IL-6 (R & D Systems) Human TNF alpha (Thermo Scientific) Ovalbumin (Sigma) BSA (Sigma) The target proteins were coated on a MaxiSorp plate (Nunc) overnight (100 μl of each target at a concentration of 10 μg/ml). ..

    Incubation:

    Article Title: Utilization of peptide phage display to investigate hotspots on IL-17A and what it means for drug discovery
    Article Snippet: Cytokines were biotinylated with EZ Link NHS-Biotin according to manufacturer’s instructions (#21336; Thermo). .. Biotinylated cytokines, 250ng/mL human IL-17A (#317-ILB; R&D Systems), 100ng/mL human IL-17C (#1234-IL; R&D Systems), 100ng/mL human IL-17E (#1258-IL; R&D Systems), and 100ng/mL human IL-17F (#1335-IL; R&D Systems) were incubated in the presence of inhibitor compounds in wash buffer at the indicated concentrations for 1hr. ..

    Recombinant:

    Article Title: IL-17C Protects Nasal Epithelium from Pseudomonas aeruginosa Infection
    Article Snippet: Interleukin-17 (IL-17) family cytokines are directly involved in host immune responses and the critical mediators for host defense against infection or inflammation.. IL-17C is highly expressed in respiratory epithelium and is induced after acute bacterial lung infection.. However, the definite function of IL-17C induced by Pseudomonas aeruginosa (PAO1) is not fully understood and our study was designed to demonstrate IL-17C-induced immune response against PAO1 infection in nasal epithelium.



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    Effect of <t>IL-17C</t> on malignant transformation in IL-17RE knockdown and overexpressed endometriotic cells (A) qPCR and western blot assay were used to measure the transfection efficiency and IL-17RE expression of si-IL-17RE in 11Z and 12Z. (B) Immunofluorescence staining reveals the effect <t>of</t> <t>rhIL-17C</t> on the expression of PCNA in IL-17RE knockdown 11Z and 12Z. (C–E) (C) Colony formation, (D) adhesion, and (E) migration and invasion were detected in parallel 11Z and 12Z cultures. (F and G) Western blot analysis was used to detect the expression of EMT-related and PI3K pathway key proteins in IL-17RE knockdown cells with or without rhIL-17C for 24 h. (H–J) (H) Immunohistological staining of PCNA, (I) colony formation, and (J) migration and invasion was detected in IL-17RE-overexpressing 11Z and 12Z with and without MOR106 treatment for 24 h. (K) Western blot analysis was used to detect the expression of EMT-related and (L) PI3K pathway key proteins in 11Z and 12Z with and without MOR106 treatment. n = 3 biological replicates. Data are represented as mean ± SEM. ∗ p < 0.05 and ∗∗ p < 0.01 for the indicated comparisons. Differences between groups were assessed using one-way ANOVA with Tukey’s post-hoc test. ns, not significant. Scale bars, 100 μm.
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    Effect of IL-17C on malignant transformation in IL-17RE knockdown and overexpressed endometriotic cells (A) qPCR and western blot assay were used to measure the transfection efficiency and IL-17RE expression of si-IL-17RE in 11Z and 12Z. (B) Immunofluorescence staining reveals the effect of rhIL-17C on the expression of PCNA in IL-17RE knockdown 11Z and 12Z. (C–E) (C) Colony formation, (D) adhesion, and (E) migration and invasion were detected in parallel 11Z and 12Z cultures. (F and G) Western blot analysis was used to detect the expression of EMT-related and PI3K pathway key proteins in IL-17RE knockdown cells with or without rhIL-17C for 24 h. (H–J) (H) Immunohistological staining of PCNA, (I) colony formation, and (J) migration and invasion was detected in IL-17RE-overexpressing 11Z and 12Z with and without MOR106 treatment for 24 h. (K) Western blot analysis was used to detect the expression of EMT-related and (L) PI3K pathway key proteins in 11Z and 12Z with and without MOR106 treatment. n = 3 biological replicates. Data are represented as mean ± SEM. ∗ p < 0.05 and ∗∗ p < 0.01 for the indicated comparisons. Differences between groups were assessed using one-way ANOVA with Tukey’s post-hoc test. ns, not significant. Scale bars, 100 μm.

    Journal: Cell Reports Medicine

    Article Title: Therapeutic targeting of interleukin-17C signaling in carcinogenesis of endometriosis

    doi: 10.1016/j.xcrm.2025.102464

    Figure Lengend Snippet: Effect of IL-17C on malignant transformation in IL-17RE knockdown and overexpressed endometriotic cells (A) qPCR and western blot assay were used to measure the transfection efficiency and IL-17RE expression of si-IL-17RE in 11Z and 12Z. (B) Immunofluorescence staining reveals the effect of rhIL-17C on the expression of PCNA in IL-17RE knockdown 11Z and 12Z. (C–E) (C) Colony formation, (D) adhesion, and (E) migration and invasion were detected in parallel 11Z and 12Z cultures. (F and G) Western blot analysis was used to detect the expression of EMT-related and PI3K pathway key proteins in IL-17RE knockdown cells with or without rhIL-17C for 24 h. (H–J) (H) Immunohistological staining of PCNA, (I) colony formation, and (J) migration and invasion was detected in IL-17RE-overexpressing 11Z and 12Z with and without MOR106 treatment for 24 h. (K) Western blot analysis was used to detect the expression of EMT-related and (L) PI3K pathway key proteins in 11Z and 12Z with and without MOR106 treatment. n = 3 biological replicates. Data are represented as mean ± SEM. ∗ p < 0.05 and ∗∗ p < 0.01 for the indicated comparisons. Differences between groups were assessed using one-way ANOVA with Tukey’s post-hoc test. ns, not significant. Scale bars, 100 μm.

    Article Snippet: Moreover, the effects of rhIL-17C (1234-IL-025, R&D Systems), anti-IL-17RE (NEUT-1237CQ, Creative biolabs, USA), MOR106 (BR2010231, Shanghai bioleaper biotechnology Co. Ltd., China) and LY294002 (HY-10108, MCE) were evaluated on cells respectively.

    Techniques: Transformation Assay, Knockdown, Western Blot, Transfection, Expressing, Immunofluorescence, Staining, Migration