Tdp-43-egfp
Tdp-43-egfp - Related Videos
13:31
Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis
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Cited by 17 •
2015
Using atomic force microscopy in combination with biopanning technology we created a negative and positive biopanning system to acquire antibodies against disease-specific protein variants present in any biological material, even at low concentrations. We were successful in obtaining antibodies to TDP-43 protein variants involved in Amyotrophic Lateral Sclerosis.
07:07
Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy
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Cited by 3 •
2021
Glucose uptake is increased in Drosophila motor neurons affected by TAR DNA binding protein (TDP-43) proteinopathy, as indicated by a FRET-based, genetically encoded glucose sensor.
07:14
Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae
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2022
We describe a protocol to induce phase transition of TAR DNA-binding protein 43 (TDP-43) by light in the spinal motor neurons using zebrafish as a model.
09:20
Perturbing Endothelial Biomechanics via Connexin 43 Structural Disruption
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Cited by 6 •
2019
Here, we present a mechanics-based protocol to disrupt the gap junction connexin 43 and measure the subsequent impact this has on endothelial biomechanics via observation of tractions and intercellular stresses.
11:43
Easy Measurement of Diffusion Coefficients of EGFP-tagged Plasma Membrane Proteins Using k-Space Image Correlation Spectroscopy
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Cited by 37 •
2014
This paper provides a step by step guide to the fluctuation analysis technique k-Space Image Correlation Spectroscopy (kICS) for measuring diffusion coefficients of fluorescently labeled plasma membrane proteins in live mammalian cells.
FAQs
EGFP supplies a fluorescent readout that makes the fusion protein visible during microscopy after excitation with suitable light. Investigators can therefore follow where the TDP-43-containing construct appears in living cells and relate fluorescence patterns to changes in localization, distribution, and aggregate formation. The tag links molecular behavior to an observable cellular signal.
Microscopy can reveal changes in localization, distribution, and aggregate formation, which represent different aspects of TDP-43 behavior. Localization concerns where the protein appears, distribution describes its spatial pattern, and aggregation reflects the formation of concentrated assemblies. Distinguishing these readouts helps characterize how cellular models respond to engineered changes or stress.
The TDP-43 portion retains interactions with RNA and cellular structures. Consequently, the fluorescence is not merely a free marker signal; it reports behavior of a tagged protein that can participate in those cellular relationships. This makes the construct useful for examining whether localization or aggregation changes occur within a cellular context where TDP-43 interactions remain relevant.
Researchers observe cells containing the fusion protein with microscopy and excite EGFP using suitable light. They then monitor fluorescence-associated changes in localization, distribution, or aggregate formation during observation. This workflow produces a visual readout of TDP-43 behavior in living cells, supporting evaluation of cellular conditions, engineered systems, or molecular interventions.
It gives a cell-based model an observable way to represent protein mislocalization and aggregation, processes associated with neurodegenerative disease. Because these changes can be monitored in living cells, the construct supports assessment of how an engineered system displays disease-relevant protein behavior. It can also provide a basis for evaluating molecular interventions designed to alter those behaviors.
Changes in fluorescence distribution can be examined while cells undergo the conditions being studied, allowing researchers to ask whether stress is accompanied by altered TDP-43 localization, distribution, or aggregate formation. In bioengineering, this links a stress-response experiment to a visible protein-level outcome and helps evaluate how engineered systems affect TDP-43 behavior under cellular stress.