Recombinant protein expression is a technique used in molecular biology and pharmaceutical production to produce proteins from recombinant DNA. This involves introducing carefully selected DNA sequences into host cells to initiate gene expression and produce the desired protein. The expressed proteins must be purified from destroyed cell parts, and this technology has broad commercial and medical applications, including the production of human growth hormone and insulin. Bacteria, fungi, and yeasts are commonly used as host cells.
Recombinant protein expression is the production of a recombinant DNA-derived protein. It is a common technique in molecular biology and pharmaceutical production of hormone substitutes. Recombinant DNA is a specific portion of a gene designed to express a single product within a host cell, driven by special chemical factors so that the right protein is expressed in large quantities. Many hormones and enzymes that have historically been derived from animal sources are now synthesized by recombinant protein expression, then harvested and refined from host cells.
To express recombinant proteins, carefully selected DNA sequences must be introduced into the host genome. Taking portions of the genetic code from one organism and inserting them into the cell nuclei of another is a form of cloning. This is done by inserting a recombinant DNA sequence coding for the desired protein into the nucleus, which initiates gene expression by transcribing it into RNA. Recombinant proteins are assembled when pieces of mRNA carrying information from DNA migrate to ribosomes from the nucleus of the cell and there they initiate the production of a protein according to a specific template.
Host cells will produce insufficient amounts of a recombinant protein unless DNA is introduced with appropriate vectors so that the right genetic information is expressed in sufficient quantity. Protein expression factors are the molecular signals that must accompany recombinant DNA as it is inserted into host cells to ensure that the target protein is overexpressed. This is the only way that recombinant protein expression can produce a substance sufficient for laboratory or pharmaceutical use.
Ribosomal protein assembly does not complete the process of protein expression because during harvesting the contents of the bacterial or yeast cells are mixed with the final product. The expressed recombinant proteins must be purified by separation from the pieces of destroyed cell parts. Sometimes a molecular tag labels the protein so it can bind to a metallic or other substance and be isolated from waste. There are several techniques, depending on factors such as the size of the protein and the complexity of the host cell.
Expression of human recombinant protein has broad commercial and medical applications. Many hormones, antibodies and enzymes were previously extracted from animal tissue or cadavers but are now being produced synthetically using recombinant DNA technology. Two particularly prominent examples are human growth hormone and insulin. Many HRTs are based on synthetic proteins, as are various tests used by molecular and cell biologists in their laboratories. In many cases, bacteria are used as host cells for simple products, while the expression of more complex recombinant proteins, especially of animal genes, can be carried out in fungi and yeasts.
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