Rat Recombinant IL17F protein, His Tag (V2LY-0526-LY9443)

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Basic Information

Expressed Host
Baculovirus-Insect Cells
Protein Species
Rat
Tag
His Tag
Protein Construction
This product is Rat Recombinant IL17F protein, His Tag consist of Amino Acid: 1-153 and predicts a molecular mass of 16.4 kDa.
Molecule Mass
16.4 kDa
Sequence
Amino Acid: 1-153
Species
Rat

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>90% as determined by SDS-PAGE.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Tris, NaCl, Glutathione, EDTA, DTT, PMSF, Glycerol
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Interleukin 17F
Function
Effector cytokine of innate and adaptive immune system involved in antimicrobial host defense and maintenance of tissue integrity (PubMed:21350122).

IL17A-IL17F signals via IL17RA-IL17RC heterodimeric receptor complex, triggering homotypic interaction of IL17RA and IL17RC chains with TRAF3IP2 adapter through SEFIR domains. This leads to downstream TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways ultimately resulting in transcriptional activation of cytokines, chemokines, antimicrobial peptides and matrix metalloproteinases, with potential strong immune inflammation (PubMed:18684971, PubMed:21350122, PubMed:11591732, PubMed:11591768, PubMed:17911633, PubMed:11574464, PubMed:28827714).

IL17A-IL17F is primarily involved in host defense against extracellular bacteria and fungi by inducing neutrophilic inflammation (By similarity).

As signature effector cytokine of T-helper 17 cells (Th17), primarily induces neutrophil activation and recruitment at infection and inflammatory sites (By similarity).

Stimulates the production of antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the entry of microbes through the epithelial barriers (By similarity).

IL17F homodimer can signal via IL17RC homodimeric receptor complex, triggering downstream activation of TRAF6 and NF-kappa-B signaling pathway (PubMed:32187518).

Via IL17RC induces transcriptional activation of IL33, a potent cytokine that stimulates group 2 innate lymphoid cells and adaptive T-helper 2 cells involved in pulmonary allergic response to fungi. Likely via IL17RC, promotes sympathetic innervation of peripheral organs by coordinating the communication between gamma-delta T cells and parenchymal cells. Stimulates sympathetic innervation of thermogenic adipose tissue by driving TGFB1 expression (By similarity).

Regulates the composition of intestinal microbiota and immune tolerance by inducing antimicrobial proteins that specifically control the growth of commensal Firmicutes and Bacteroidetes (By similarity).
Biological Process
Adaptive immune response Source: UniProtKB-KW
Cartilage development Source: UniProtKB
Defense response to Gram-negative bacterium Source: Ensembl
Defense response to Gram-positive bacterium Source: Ensembl
Inflammatory response Source: UniProtKB-KW
Innate immune response Source: UniProtKB-KW
Interleukin-17-mediated signaling pathway Source: UniProtKB
Negative regulation of angiogenesis Source: UniProtKB
Positive regulation of antimicrobial peptide production Source: Ensembl
Positive regulation of chemokine (C-X-C motif) ligand 1 production Source: UniProtKB
Positive regulation of cytokine production Source: UniProtKB
Positive regulation of cytokine production involved in inflammatory response Source: Ensembl
Positive regulation of interleukin-6 production Source: UniProtKB
Positive regulation of lymphotoxin A production Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: Ensembl
Regulation of granulocyte macrophage colony-stimulating factor production Source: UniProtKB
Regulation of interleukin-2 production Source: UniProtKB
Regulation of interleukin-6 production Source: UniProtKB
Regulation of interleukin-8 production Source: UniProtKB
Regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
Cellular Location
Secreted
Involvement in disease
Candidiasis, familial, 6 (CANDF6):
A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.

Tam, H. K. J., Robinson, P. C., & Nash, P. (2022). Inhibiting IL-17A and IL-17F in rheumatic disease: Therapeutics help to elucidate disease mechanisms. Current Rheumatology Reports, 24(10), 310-320.

Braga, M., Lara-Armi, F. F., Neves, J. S. F., Rocha-Loures, M. A., Terron-Monich, M. D. S., Bahls-Pinto, L. D., ... & Visentainer, J. E. L. (2021). Influence of IL10 (rs1800896) polymorphism and TNF-α, IL-10, IL-17A, and IL-17F serum levels in ankylosing spondylitis. Frontiers in immunology, 12, 653611.

Iznardo, H., & Puig, L. (2021). Dual inhibition of IL-17A and IL-17F in psoriatic disease. Therapeutic Advances in Chronic Disease, 12, 20406223211037846.

Adams, R., Maroof, A., Baker, T., Lawson, A. D., Oliver, R., Paveley, R., ... & Griffiths, M. (2020). Bimekizumab, a novel humanized IgG1 antibody that neutralizes both IL-17A and IL-17F. Frontiers in Immunology, 11, 1894.

Goepfert, A., Lehmann, S., Blank, J., Kolbinger, F., & Rondeau, J. M. (2020). Structural analysis reveals that the cytokine IL-17F forms a homodimeric complex with receptor IL-17RC to drive IL-17RA-independent signaling. Immunity, 52(3), 499-512.

Gao, S., Mao, C., Cheng, J., Deng, Q., & Sheng, W. (2020). Association of IL‐17A‐197G/A and IL‐17F‐7488T/C polymorphisms and osteoarthritis susceptibility: A meta‐analysis. International Journal of Rheumatic Diseases, 23(1), 37-46.

Burns, L. A., Maroof, A., Marshall, D., Steel, K. J., Lalnunhlimi, S., Cole, S., ... & Taams, L. S. (2020). Presence, function, and regulation of IL‐17F‐expressing human CD4+ T cells. European Journal of Immunology, 50(4), 568-580.

Chen, Y., Chen, Y., Cao, P., Su, W., Zhan, N., & Dong, W. (2020). Fusobacterium nucleatum facilitates ulcerative colitis through activating IL‐17F signaling to NF‐κB via the upregulation of CARD3 expression. The Journal of pathology, 250(2), 170-182.

Glatt, S., Baeten, D., Baker, T., Griffiths, M., Ionescu, L., Lawson, A. D., ... & Shaw, S. (2018). Dual IL-17A and IL-17F neutralisation by bimekizumab in psoriatic arthritis: evidence from preclinical experiments and a randomised placebo-controlled clinical trial that IL-17F contributes to human chronic tissue inflammation. Annals of the rheumatic diseases, 77(4), 523-532.

Tang, C., Kakuta, S., Shimizu, K., Kadoki, M., Kamiya, T., Shimazu, T., ... & Iwakura, Y. (2018). Suppression of IL-17F, but not of IL-17A, provides protection against colitis by inducing Treg cells through modification of the intestinal microbiota. Nature Immunology, 19(7), 755-765.

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For research use only. Not intended for any clinical use.

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