IL 17A/F Human
Greater than 95.0% as determined by SDS-PAGE.
Description
The IL-17A/F Human is purified by proprietary chromatographic techniques.
Product Specs
A protein solution containing 0.1% TFA was filtered through a 0.2µm filter before lyophilization to obtain IL-17A/F.
For reconstitution of the lyophilized Interleukin Human IL-17A/F, it is recommended to dissolve it in sterile water at a concentration of 0.1mg/ml. Further dilutions can be prepared using other aqueous solutions.
The purity of the product, as determined by SDS-PAGE analysis, is greater than 95.0%.
The biological activity, assessed by measuring IL-6 production from mouse 3T3 cells, is 3.2ng/ml, which corresponds to 3.1x105 units per mg of protein.
MIVKAGITIP RNPGCPNSED KNFPRTVMVN LNIHNRNTNT NPKRSSDYYN RSTSPWNLHR NEDPERYPSV IWEAKCRHLG CINADGNVDY HMNSVPIQQE ILVLRREPPH CPNSFRLEKI LVSVGCTCVT PIVHHVA.
MRKIPKVGHT FFQKPESCPP VPGGSMKLDI GIINENQRVS MSRNIESRST SPWNYTVTWD PNRYPSEVVQ AQCRNLGCIN AQGKEDISMN SVPIQQETLV VRRKHQGCSV SFQLEKVLVT VGCTCVTPVI HHVQ.
Product Science Overview
Interleukin-17A/F (IL-17A/F) is a heterodimeric cytokine composed of two members of the IL-17 family: IL-17A and IL-17F. These cytokines play a crucial role in the immune system, particularly in the regulation of inflammatory responses. The human recombinant form of IL-17A/F is produced using advanced biotechnological methods, allowing for its use in research and therapeutic applications.
The IL-17A/F heterodimer is a cystine-linked molecule consisting of one subunit of IL-17A and one subunit of IL-17F. The recombinant human IL-17A/F is typically produced in various expression systems, including E. coli and Chinese Hamster Ovary (CHO) cells. The heterodimer is non-glycosylated when produced in E. coli and glycosylated when produced in mammalian cells .
The molecular weight of the IL-17A/F heterodimer is approximately 30.7 kDa when produced in E. coli and around 38 kDa when produced in mammalian cells due to glycosylation . The recombinant protein is purified using proprietary chromatographic techniques to ensure high purity and bioactivity .
IL-17A/F is primarily produced by Th17 cells and γδ T cells. It functions as a bridge between adaptive and innate immunity by stimulating the production of pro-inflammatory cytokines and neutrophil chemoattractants . This cytokine plays a significant role in the body’s defense against bacterial and fungal infections and is also involved in the pathogenesis of various inflammatory and autoimmune diseases .
Recombinant human IL-17A/F is produced using different expression systems. In E. coli, the protein is expressed as a non-glycosylated polypeptide chain, while in CHO cells, it is expressed as a glycosylated protein . The recombinant protein is purified to a high degree of purity, typically greater than 95% as determined by SDS-PAGE . The endotoxin levels are kept below 1.0 EU per 1 μg of protein to ensure its suitability for research and therapeutic applications .
The recombinant IL-17A/F heterodimer is widely used in research to study its role in immune responses and its potential therapeutic applications. It is used in various assays to measure its bioactivity, such as its ability to induce IL-6 secretion by NIH-3T3 mouse embryonic fibroblast cells . The recombinant protein is also used in the development of therapeutic agents targeting IL-17A/F for the treatment of inflammatory and autoimmune diseases .
