Recombinant Fusion Protein
Recombinant Fusion Protein - Related Videos
07:35
Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
0 Views •
Cited by 48 •
2014
Elastin-like polypeptides are stimulus-responsive biopolymers with applications ranging from recombinant protein purification to drug delivery. This protocol describes the purification and characterization of elastin-like polypeptides and their peptide or protein fusions from Escherichia coli using their lower critical solution temperature phase transition behavior as a simple alternative to chromatography.
19:23
Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation
0 Views •
Cited by 9 •
2019
Here, we present the detailed procedure of a recently developed protease assay platform utilizing N-terminal hexahistidine/maltose-binding protein and fluorescent protein-fused recombinant substrates attached to the surface of nickel-nitrilotriacetic acid magnetic agarose beads. A subsequent in-gel analysis of the assay samples separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis is also presented.
08:13
A Cre-Lox P Recombination Approach for the Detection of Cell Fusion In Vivo
0 Views •
Cited by 11 •
2012
A method to track cell fusion in living organisms over time is described. The approach utilizes Cre-LoxP recombination to induce luciferase expression upon cell fusion. The luminescent signal generated can be detected in living organisms using biophotonic imaging systems with a sensitivity of detection of ˜1,000 cells in peripheral tissues.
09:27
Generation of Fluorescent Protein Fusions in Candida Species
0 Views •
Cited by 6 •
2017
PCR-mediated gene modification can be used to generate fluorescent protein fusions in Candida species, which facilitates visualization and quantitation of yeast cells and proteins. Herein, we present a strategy for constructing a fluorescent protein fusion (Eno1-FP) in Candida parapsilosis.
01:24
Tagging and Fusion Proteins
0 Views •
2023
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
FAQs
A flexible peptide linker separates the joined protein domains and can help each domain preserve its intended function. By providing spacing between the regions, it supports the combined molecule’s structural design rather than forcing the domains into direct contact. This feature is important when scientists want one product to retain both target-recognition and biological activities.
The recombinant DNA construct places the desired coding sequences together in an arrangement that the host cell can use to produce the combined protein. Its design determines which protein regions are joined and whether a linker separates them. Consequently, construct planning is central to obtaining a molecule with the intended combination of recognition, activity, or other properties.
Expression produces the engineered protein in a host cell, while purification isolates it from other cellular components. Characterization then examines the resulting product to determine whether the intended fused molecule was obtained and whether its properties are consistent with the design. Together, these stages connect genetic construction with evaluation of a usable research or medical product.
Fusing domains can combine functions that would otherwise reside in separate proteins. For example, one region may provide target recognition while another contributes biological activity, allowing the resulting molecule to perform both roles. This modular strategy gives scientists a way to design proteins with properties suited to particular medical objectives, rather than relying on a single native protein.
Medical applications include drug development, targeted therapies, vaccine design, and diagnostic assays. Their value comes from combining protein functions within one engineered product, such as recognition of a desired target together with a biological effect. The same design approach can therefore support both therapeutic development and tools that detect or investigate medically relevant targets.
Recombinant fusion proteins also serve as experimental tools for studying protein interactions and disease mechanisms. Their joined domains can help researchers examine how recognition and biological activity operate together in a controlled engineered molecule. This provides a research context for understanding disease-related processes while also informing the design of therapies, vaccines, and diagnostic systems.