Proteins often referred to as the powerhouse in biological systems, are involved in several bodily functions of a cell, such as a gene expression, cell development, proliferation, nutrition, apoptosis, and intercellular communication. DNA stores the basic scaffold for protein synthesis, which serves as a scaffold for highly controlled transcriptional activities to form messenger RNA.
The information captured by mRNA is then converted into specific patterns of amino acids, resulting in a protein. Proteins follow the same two-step process in all species: DNA first converts to RNA. Proteins are then synthesized from RNA. Institutions such as Shenandoah Biotech offers human SCF. Here’s everything you need to know about them.
What Exactly are Recombinant Proteins?
Recombinant proteins, being modified native proteins, are produced in various methods to maximize the production of proteins, alter gene sequences, and produce valuable commodities. These proteins are encoded by recombinant DNA cloned in an expression system supporting mRNA translation and gene expression. Using recombinant DNA tech to alter the gene can result in expressing mutant proteins.
Production of Recombinant Proteins
The production of recombinant proteins begins at the genetic level. Human genes can be highly complex and usually have noncoding DNA regions, i.e., introns. The protein-coding sequence is extracted and copied into an expressing plasmid vector. Many recombinant proteins for therapy are derived from humans but are synthesized in organisms such as yeast, bacteria, and animal cells.
The production of recombinant proteins for academic purposes generally depends on the cost-effectiveness, convenience, and speed of the process combined with sufficient quantities of the product. Therefore, intron-free forms of genes are usually products of the conversion of mRNA to cDNA. Since cDNA lacks control regions, expression vectors contain terminator sequences and ribosome-binding regions. Proteins co-expressed in bacteria don’t contain post-translational modifications such as glycosylation and phosphorylation. Eukaryotic expression methods are required for this purpose.
Most recombinant proteins require protein modifications, e.g., glycosylation, which is exclusive to eukaryotic cells. Insect cells, mammalian cell cultures, and yeast provide such types of post-translation changes. Effective transient transfection techniques have been developed over the past decade. Cell lines derived from HEK293 are necessary for the brief synthesis of proteins. Currently, most recombinant therapeutic proteins are produced in mammalian cells because mammalian cells can generate high-quality proteins that are identical to organic proteins. In addition, several approved recombinant therapeutic proteins are produced in E.coli because it has well-formed genetics, explosive growth, and high production yield.
Applications of Recombinant Proteins
Here are some uses of recombinant proteins;
1. Research in Medicine to Understand Wellness and Disease
The study of protein-protein interactions requires recombinant proteins as practical tools. Both types play essential roles in cellular processes. Protein interactions can be broadly divided into transient and stable interactions. Currently, RP microarrays are popular as a method to study protein-protein relationships. In this method, researchers first load a slide with several immobilized proteins. Then they treat the fall with different molecules and explore how the two substances interact with each other. Scientists have used this method to study the interaction of proteins with nucleic acids, small molecules, peptides, enzymes, proteins, and lipids. As a result, a higher throughput could be achieved.
Recombinant proteins are necessary for the development of enzymatic experiments. ELISA, immunohistochemistry (IHC), and Western blot are a few of the analytical methods used in the laboratory to demonstrate the efficacy of recombinant proteins. For example, recombinant proteins serve as ELISA baselines and positive regulators in Western blots. They are also combined in immunohistochemistry with perfectly matched antibody pairs. When studying how cells respond to different types of stress and disease, recombinant proteins are helpful tools to have on hand. Administering peptides and recombinant proteins to experimental disease models helps researchers find innovative treatments.
2. Recombinant DNA- Derived Proteins for Biotherapy
The dysfunction of specific proteins is either wholly or partially responsible for most human diseases. Proteins used for therapeutic purposes are essential for treating various diseases such as cancer, diabetes, infectious diseases, anemia, and hemophilia.
Genetically engineered human proteins significantly influence the therapeutic drug market. Hormones, antibodies, interleukins, anticoagulants, Fc fusion proteins, and enzymes are various protein therapeutics. The hepatitis B vaccine, for example, is one of the FDA-approved RP vaccines. It is designed to protect against infection with all recognized variants of the hepatitis B virus.
Doctors use recombinant proteins to treat diseases such as dwarfism, neutropenia, diabetes, heart attack, anemia, stroke, rheumatoid arthritis, etc. When looking for recombinant or native proteins to use in various areas, it is critical to turn to vetted and specialized sources that have undergone functional testing and maintain the highest quality throughout the manufacturing process.