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Certain strains of S. coelicolor can used for heterologous protein expression.
These compounds can range from heterologous proteins and amino-acids to vitamins.
The heterologous protein is inserted at the passenger domain.
Scaffolds are used to display the heterologous protein on the bacterial cell surface.
Under these conditions, L. plantarum strains producing high levels of heterologous proteins have been found to remain highly competitive.
The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together.
The infection of cells with this altered virus elicits a specific lactogenic immune response against the heterologous protein.
Screening is used to find the apparent affinities of heterologous proteins displayed on the bacterial cell surface for target proteins.
Another method of heterologous protein fusion is fusion with fimbriae/flagella, which are filamentous protrusions on the cell surface.
The display of heterologous proteins on the bacterial cell surface normally requires the fusion of the protein with a surface protein, called a scaffold.
As a yeast, it shares the advantages of molecular and genetic manipulations with Saccharomyces, and it has the added advantage of 10- to 100-fold higher heterologous protein expression levels.
Expression of heterologous proteins by viruses is the basis of several manufacturing processes that are currently being used for the production of various proteins such as vaccine antigens and antibodies.
E. coli is a very versatile host for the production of heterologous proteins, and various protein expression systems have been developed which allow the production of recombinant proteins in E. coli.
Considered a very versatile host for the production of heterologous proteins, researchers can introduce genes into the microbes using plasmids, allowing for the mass production of proteins in industrial fermentation processes.
Information on the size of the cell can be obtained by the scattering of light and if binding of the heterologous protein with the target protein/cell has occurred, there will be more fluorescence emitted.
Mendozavega O, Sabatie J, Brown SW: Industrial-Production of Heterologous Proteins by Fed-Batch Cultures of the Yeast Saccharomyces-Cerevisiae.
If the unique C-terminal 35 amino acid sequence of sα i2 functions as a Golgi targeting signal, it is important to test whether it is sufficient to target a heterologous protein to intracellular membranes.
Once the heterologous protein has been fused with the bacterial cell surface protein, it is exposed to either an enzyme, a cell (expressing a target protein) or an antibody (usually fluorescently tagged), depending on the application of the experiment.
The expression host of choice for the expression of many proteins is Escherichia coli as the production of heterologous protein in E. coli is relatively simple and convenient, as well as being rapid and cheap.
To determine whether the hypervariable domain of Rab24 was sufficient to promote the formation of inclusion bodies when fused to a heterologous protein, we prepared fusion constructs with enhanced green fluorescent protein (EGFP) containing either full-length Rab24(D123I) or just the Rab24 C-terminal domain.
Previously acquired immunity to a viral vector such as vaccinia may influence its efficacy in inducing immunity against heterologous proteins being delivered [ 16 17 18 19 ] and it may be wise to provide physicians with HIV vaccines based on a variety of vectors to handle a variety of clinical situations.