IL17F Human, sf9

Interleukin 17F Human Recombinant, sf9
Cat. No.
BT9938
Source
Sf9, Baculovirus cells.
Synonyms

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1. 

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

IL17F produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (31-163 a.a.) and having a molecular mass of 16kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa). IL17F is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

IL-17F, identified by the accession number Q96PD4, is a cytokine with similarities to IL-17 in its amino acid sequence. Produced by activated T cells, IL-17F has been found to stimulate the production of various other cytokines such as IL6, IL8, and CSF2/GM-CSF. Furthermore, IL-17F demonstrates inhibitory effects on the formation of new blood vessels (angiogenesis) in endothelial cells, while simultaneously promoting these cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F also induces stromal cells to produce cytokines involved in inflammation and blood cell formation. Notably, IL-17F gene expression is elevated in the intestines of individuals with active Crohn's disease. Both IL-17A and IL-17F alleles play independent roles in influencing susceptibility to and the pathological characteristics of ulcerative colitis. Genetic variations in IL-17F and MIF genes are significantly linked to the development of functional dyspepsia. The initiation of the IL-17F/IL-17R signaling cascade relies on the ubiquitination of the receptor by TRAF6. IL-17F triggers the expression of IFN-gamma-inducible protein 10 (IP-10) through the activation of the Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.

Description

IL17F, produced using Sf9 insect cells infected with a baculovirus expression system, is a single-chain polypeptide that has undergone glycosylation. It consists of 142 amino acids (specifically, amino acids 31 to 163) and has a molecular mass of 16 kDa. When analyzed using SDS-PAGE, it appears as a band in the range of approximately 18-28 kDa. This IL17F protein is engineered with a 9-amino acid Histidine tag located at the C-terminus to facilitate purification. The protein is purified using specialized chromatographic methods.

Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation

The IL17F protein solution is supplied at a concentration of 0.5 mg/ml. The solution is formulated in a buffer consisting of Phosphate Buffered Saline (pH 7.4), 20% glycerol, and 1mM DTT.

Stability
For short-term storage (up to 2-4 weeks), the IL17F protein solution should be kept refrigerated at 4°C. For longer storage, it is recommended to store the solution frozen at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein such as HSA or BSA to a final concentration of 0.1%. Repeated cycles of freezing and thawing should be avoided to maintain protein integrity.
Purity

The purity of the IL17F protein is greater than 95.0% as determined by SDS-PAGE analysis.

Synonyms

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1. 

Source
Sf9, Baculovirus cells.
Amino Acid Sequence

ADPRKIPKVG HTFFQKPESC PPVPGGSMKL DIGIINENQR VSMSRNIESR STSPWNYTVT WDPNRYPSEV VQAQCRNLGC INAQGKEDIS MNSVPIQQET LVVRRKHQGC SVSFQLEKVL VTVGCTCVTP VIHHVQHHHH HH.

Product Science Overview

Introduction

Interleukin 17F (IL-17F) is a pro-inflammatory cytokine that plays a crucial role in the immune response. It is part of the interleukin 17 family, which includes several other cytokines involved in inflammation and host defense. IL-17F is primarily produced by T helper 17 (Th17) cells, but it can also be secreted by a variety of other cell types, including innate immune cells and epithelial cells .

Gene and Protein Structure

The IL17F gene is located on chromosome 6p12 in humans . The gene encodes a protein that can form either homodimers or heterodimers with other members of the interleukin 17 family. The recombinant form of IL-17F produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids, with a molecular mass of approximately 16 kDa . This recombinant protein is often tagged with a His tag at the C-terminus to facilitate purification .

Biological Function

IL-17F is involved in the development of inflammation and the host defense against infections. It induces the expression of genes that encode other pro-inflammatory cytokines, such as tumor necrosis factor (TNF), interleukin 1 (IL-1), and interleukin 6 (IL-6) . Additionally, IL-17F promotes the production of chemokines like CXCL1, CXCL5, and interleukin 8 (IL-8), which are essential for neutrophil recruitment and inflammation .

The target cells of IL-17F include epithelial cells, fibroblasts, keratinocytes, synoviocytes, and endothelial cells . By binding to its receptor complex, IL-17RA-IL-17RC, IL-17F triggers signaling pathways that lead to the activation of NF-kappa-B and MAP kinase pathways, resulting in the transcriptional activation of various cytokines, chemokines, antimicrobial peptides, and matrix metalloproteinases .

Clinical Relevance

IL-17F has been implicated in several inflammatory and autoimmune diseases. Elevated levels of IL-17F are often observed in conditions such as psoriasis, rheumatoid arthritis, and inflammatory bowel disease . Due to its role in promoting inflammation, IL-17F is a potential therapeutic target for treating these diseases.

Recombinant IL-17F (sf9)

The recombinant form of IL-17F produced in Sf9 Baculovirus cells is used in various research applications to study its biological functions and potential therapeutic uses. This recombinant protein is glycosylated and has a molecular mass of approximately 16 kDa . It is purified using proprietary chromatographic techniques to ensure high purity and activity .

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