Dengue Envelope-3 22kDa
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Description
Dengue Envelope ST3 is a dengue antigen specially designed for ELISA test, this 22 kDa recombinant peptide contains important epitopes for dengue IgG & IgM antibody recognition and is fused with 6-His fusion partner.
Product Specs
Purified by proprietary chromatographic technique.
Product Science Overview
Dengue virus (DENV) is a mosquito-borne virus that poses a significant global health threat, with approximately 390 million infections annually . There are four distinct serotypes of the dengue virus, each capable of causing dengue fever. The Dengue Virus Subtype-3 (DENV-3) is one of these serotypes.
The envelope (E) protein of the dengue virus is a key structural component that plays a crucial role in the virus’s ability to infect host cells. The E protein is involved in the virus’s attachment to and entry into host cells. The 22kDa recombinant form of the DENV-3 envelope protein is a genetically engineered peptide designed for research and diagnostic purposes .
The recombinant DENV-3 envelope protein is typically produced using bacterial expression systems, such as Escherichia coli (E. coli). The protein is purified using proprietary chromatographic techniques to ensure high purity, often exceeding 95% as determined by PAGE (polyacrylamide gel electrophoresis) with Coomassie staining . The purified protein is formulated in phosphate-buffered saline (PBS) at pH 7.4 and is stable at 4°C for up to one week, but should be stored below -18°C to prevent freeze-thaw cycles .
The 22kDa recombinant DENV-3 envelope protein is primarily used in immunoassays, such as ELISA (enzyme-linked immunosorbent assay), to detect dengue-specific antibodies (IgG and IgM) in patient samples . This makes it a valuable tool for both diagnostic and research purposes. Additionally, the protein has potential applications in vaccine development and as a target for neutralizing therapeutic antibodies .
Recent studies have focused on optimizing the production of the DENV-3 envelope protein in various expression systems, including yeast (Pichia pastoris) and insect cells . These efforts aim to improve the yield and quality of the recombinant protein, making it more accessible for research and industrial applications. For instance, the use of casamino acids in the culture media has been shown to significantly enhance the secretion of the DENV-3 envelope protein in Pichia pastoris .
