Analytical Data
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Gene name
ALS
- Application
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Alternative Names
Acetohydroxy-acid synthase Protein CHLORSULFURON RESISTANT 1
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Species
Arabidopsis thaliana
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17597
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Expression Region
98-670aa
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Molecular Weight
64.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disorder characterized by the degeneration of motor neurons, leading to muscle weakness and atrophy. The underlying mechanisms of ALS are not yet fully understood, but genetic factors, protein aggregation, and neuroinflammation have been implicated in its pathogenesis. Recent research has focused on the role of protein aggregates, particularly the misfolded forms of proteins such as TDP-43 and FUS, which are commonly found in the affected neurons of ALS patients. The study of recombinant proteins has emerged as a vital tool in understanding the molecular basis of ALS. By producing and analyzing these proteins in vitro, researchers can investigate their structural properties, aggregation tendencies, and toxic effects on neuronal cells. This research not only aids in elucidating the pathophysiological processes of ALS but also paves the way for the development of potential therapeutic strategies aimed at preventing protein misfolding and promoting cellular resilience. Advances in techniques such as cryo-electron microscopy and high-throughput screening are facilitating deeper insights into protein interactions and aggregation pathways, which may ultimately lead to novel treatment options for ALS. Understanding the role of ALS-related recombinant proteins is crucial for uncovering the disease mechanisms and identifying targets for drug development.
