Human IL17F (Interleukin-17F) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-04153P
SDS-PAGE analysis of Human IL17F (Interleukin-17F) - Recombinant Protein, CAT
SDS-PAGE analysis of Human IL17F (Interleukin-17F) - Recombinant Protein, CAT# BLT-04153P, showing >85% purity under 15% SDS-PAGE (Reduced)

Human IL17F (Interleukin-17F) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-04153P
Regular price $595.00 Sale price $445.00Save $150
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Pack Size Price (USD)
500 µg $1,030 (Fall Promotion)
1 mg $1,870 (Fall Promotion)

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Product Overview

Product Name Recombinant Human Interleukin-17F/INHAProtein (IL17F) Protein
Product Overview This recombinant human Interleukin-17F/INHAprotein (IL17F) protein includes amino acids 31-163aa of the target gene is expressed in HEK293 Cells.The protein is supplied in lyophilized form and formulated in phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5% trehaloseprior to lyophilization.
Target Uniprot Id Q96PD4
Recommended Name Interleukin-17F
Gene Name IL17F
Synonyms Interleukin-17F; IL-17F; Cytokine ML-1; Interleukin-24; IL-24; IL17F; IL24
Species Human
Predicted Molecular Mass 16.0 kDa
Expression System Mammalian Cell
Expression Range 31-163aa
Tag C-6His
Purity >85%
Formulation Lyophilized
Buffer Phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5%Trehalose
Storage Condition 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Reconstitution Instruction Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Applications Positive Control; Immunogen; SDS-PAGE; WB
Research Area Immunology, Cancer
Target Function Effector cytokine of innate and adaptive immune system involved in antimicrobial host defense and maintenance of tissue integrity. 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. IL17A-IL17F is primarily involved in host defense against extracellular bacteria and fungi by inducing neutrophilic inflammation. As signature effector cytokine of T-helper 17 cells (Th17), primarily induces neutrophil activation and recruitment at infection and inflammatory sites. Stimulates the production of antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the entry of microbes through the epithelial barriers. IL17F homodimer can signal via IL17RC homodimeric receptor complex, triggering downstream activation of TRAF6 and NF-kappa-B signaling pathway. 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. Regulates the composition of intestinal microbiota and immune tolerance by inducing antimicrobial proteins that specifically control the growth of commensal Firmicutes and Bacteroidetes.
Subcellular Location Secreted.
Protein Family IL-17 family
Associated Diseases Candidiasis, familial, 6 (CANDF6)
Tissue Specificity Expressed in T-helper 1 and T-helper 2 cells, basophils and mast cells.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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