afg1l
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Human | AFG1L-5649H | Recombinant Human AFG1L Protein, Myc/DDK-tagged, C13 and N15-labeled | HEK293T | Myc/DDK | ||
Mouse | Afg1l-1548M | Recombinant Mouse Afg1l Protein, Myc/DDK-tagged | HEK293T | Myc/DDK |
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Q&As (10)
Ask a questionGenetic variations or mutations in the gene encoding AFG1L protein may impact its expression or function, influencing mitochondrial dysfunction or disease susceptibility.
The expression of AFG1L protein is regulated by specific factors and signaling pathways.
AFG1L protein contributes to cellular processes such as energy metabolism, oxidative stress response, or mitochondrial dynamics, and the underlying molecular mechanisms are currently being investigated.
Various experimental techniques or assays, such as mitochondrial respiration assays, electron microscopy, or gene knockout models, have been used to study the functional significance of AFG1L protein.
AFG1L protein may interact with specific molecules or participate in protein complexes, which have functional implications in cellular processes.
Post-translational modifications and regulatory mechanisms may modulate the activity or stability of AFG1L protein.
The subcellular localization of AFG1L protein can be experimentally determined using techniques such as immunofluorescence microscopy or subcellular fractionation.
AFG1L protein holds potential as a target for modulating mitochondrial function or treating mitochondrial disorders, and further research is needed to explore its implications for therapeutic interventions.
AFG1L protein plays a role in mitochondrial function or quality control, and its function can be investigated using techniques like mitochondrial respiration assays or electron microscopy.
Dysregulation or dysfunction of AFG1L protein can disrupt mitochondrial homeostasis, impair cellular energetics, and contribute to disease development.
Customer Reviews (3)
Write a reviewElucidating protein-protein interactions in autophagy flux for cellular homeostasis.
Deciphering protein-protein interactions in mitochondrial dysfunction for metabolic disorders.
Probing protein-protein interactions in neuronal development for synaptic connectivity.
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