Protein of all recombinant therapeutic proteins are produced in

 

Protein expression is a form of journey from DNA because DNA is
carry important codes that will be translated into functional proteins.
Generally, the protein production inside the cells begin with the transcription
and translation process but in laboratory practical, we can control the
expression by genetically engineered our desired protein through the gene of
interest. Hence, we can formulate them in drug forms and other but to do that
we need to produce the protein in huge amount in very tiny amount of time and
low expense. So that, we rely on the technology known as recombinant DNA using
expression system such bacteria to produce our desired protein. Previously,
people used to produce proteins directly using organic sources for an example
the insulin that we get from pancreatic cell of the cows. Unfortunately, people
easily get infected to some disease like mad cow disease. Therefore, due to
that cross-contamination, new alternative using recombinant DNA technology in
the expression system.

As we all know, recombinant protein expression is likely quite
simple as DNA that encoding target protein is cloned in an expression vector.
Later, it is then being introduced into host cells and the protein synthesis of
the cell machinery produces the desired protein. Mostly, protein are expressed and
may be produced intracellular or be secreted using the suitable expression
vectors. Therefore, the basis of the recombinant DNA construction is depend on
the factors such as the vector consist of the inducible promoter, suitable expression
host and others. While the expression of the protein, all protein were
expressed, thus using the correct expression vector will distinguish the target
protein from other fusion protein system by its ability to separate a
recombinant protein from the affinity tag without the uses of protease.

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Recently, recombinant protein have been widely used such in medical
and therapeutic, research, biotechnology and others. It is based on their
functions in the body, proteins can be divided into different categories, such
as antibody, enzyme, messenger, structural component, and transport and storage
protein. Currently, most of all recombinant therapeutic proteins are produced
in mammalian cells because mammalian cells are capable of producing
high-quality proteins similar to the naturally occurring ones. In addition,
many approved recombinant therapeutic proteins are generated in Escherichia
coli due to its well-characterized genetics, rapid growth, and high-yield
production. It is also a functional bacterium that has been remarked its
functionality by drug regulatory authorities and grows rapidly to a high
density on its sole of carbon source (L. Briand et. Al 2015). Besides, in the
production of insulin,

Besides, fundamental principle of an organisms can be resolved by
the recombinant protein in research area. As example, these molecules can be
used to identify the position of encoded protein by a specific gene and
discover the function of other genes such as cell signalling, metabolisms,
growth, protein modification and others. Therefore, it make the recombinant
protein widely used in molecular biology, cell biology, biophysical studies and
many other research fields.

Moreover, in biotechnology, recombinant protein are a useful tools
in understanding protein-protein interaction as they can be proven their
performance in many laboratory techniques. Such in ELISA and Western Blot,
recombinant protein molecules develop enzymatic assays and can conjugate with
specific antibody pair. Other than that, recombinant protein also widely used
in food production, agriculture and industry. For example, lactic acid
bacteria for the production of fermented foods such yougurt and also being engineered
for the expression of the recombinant protein. This had improved widely
application such improving human, animal digestion and nutrition.

Escherichia coli
expression can cause by several factors that yield high recombinant protein
expression. One of the commonly used in Escherichia coli expression
system is the inducible T7 RNA polymerase induced usually by Isopropyl ?-D-1-thiogalactopyranoside,
IPTG. However, there are some strategies have been developed in order to
improve expression of recombinant protein based on un-induced expression of the
bacterial system and others. Despite of these strategies had been proved to
yield high protein expression in bacterial system, but there are also some
common problem that might occur. In this review, the discussion will focus on strategies
for recombinant protein expression in bacterial system that may influenced by
two elements which are inducible and self-inducible protein expression, and
their advantages and challenges.