als3
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Yeast | ALS3-2175Y | Recombinant Yeast ALS3 Protein (918-1119 aa), His-B2M-Myc-tagged | E.coli | His/B2M/Myc | 918-1119 aa |
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Q&As (10)
Ask a questionALS3 contributes to the pathogenesis of ALS through multiple mechanisms, including mitochondrial dysfunction, impaired protein homeostasis, and dysregulated signaling pathways.
ALS3 influences mitochondrial function and dynamics, affecting processes such as mitochondrial respiration, ATP production, or mitochondrial fission and fusion.
Therapeutic interventions targeting ALS3 or its associated pathways hold promise for treating ALS and related neurodegenerative disorders by modulating mitochondrial function, protein homeostasis, or downstream signaling pathways implicated in disease pathology.
ALS3 contains functional domains and motifs, such as RNA-binding domains, prion-like domains, or regions involved in protein-protein interactions, which play a role in its molecular functions.
ALS3 expression is altered during disease progression, with increased levels in affected tissues or specific cell types. Factors such as cellular stress, inflammation, or genetic mutations can regulate ALS3 expression.
ALS3 regulates downstream signaling pathways, including those involving kinases, transcription factors, or inflammatory mediators, contributing to neuroinflammation, oxidative stress, or neuronal death.
ALS3 interacts with various proteins, such as chaperones, RNA-binding proteins, or components of the ubiquitin-proteasome system, forming dynamic protein complexes that modulate its cellular functions.
The enzymatic activities of ALS3 are not well-characterized, and further studies are needed to determine its potential enzymatic functions and identify its substrates or targets.
ALS3 is involved in the regulation of protein homeostasis, including protein folding, clearance of misfolded proteins, and prevention of protein aggregation.
ALS3 shows a predominantly cytoplasmic localization, with potential accumulation in specific subcellular compartments, such as stress granules or mitochondria, under certain conditions.
Customer Reviews (3)
Write a reviewReliable detection of protein post-translational modifications.
Compatibility with various protein analysis techniques (e.g., mass spectrometry).
High assay sensitivity without signal saturation.
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