Analytical Data
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Gene name
FUS
- Application
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Alternative Names
FUS；TLS；RNA-binding Protein FUS
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35637
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Expression Region
1-526aa
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AA Sequence
MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY
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Molecular Weight
60.9 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
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Protein Description
FUS (Fused in Sarcoma) is a DNA/RNA-binding protein that plays a crucial role in various cellular processes, including transcription regulation, RNA processing, and stress response. Its involvement in the development of several neurodegenerative diseases, particularly amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), has drawn significant research interest. Mutations in the FUS gene can lead to the mislocalization of the protein and the formation of pathological aggregates, disrupting cellular function and contributing to neurodegeneration. Studies have revealed that FUS interacts with RNA and DNA, influencing spliceosomal assembly and the maintenance of genomic integrity. As a result, researchers have focused on developing recombinant FUS proteins to better understand its structure-function relationships and the molecular mechanisms underlying its role in health and disease. The generation of FUS recombinant proteins has enabled scientists to investigate the effects of specific mutations and post-translational modifications, while also providing tools for studying FUS-related protein aggregation in vitro. This research is essential for identifying potential therapeutic targets and strategies aimed at mitigating the effects of FUS-related pathologies. Moreover, understanding the biological functions of FUS could lead to novel insights into RNA metabolism and the regulation of gene expression, offering broader implications for cellular biology and neurobiology.
