Analytical Data
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Gene name
FUS
- Application
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Alternative Names
RNA-binding protein FUS; 75 kDa DNA-pairing protein; Oncogene FUS; Oncogene TLS; POMp75; Translocated in liposarcoma protein; TLS
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Species
Human
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Source
E. coli
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Tag
N-10*His;C-Myc
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P35637-1
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Expression Region
M1-Y526
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Protein Length
Full Length of Isoform-1
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Molecular Weight
68-70 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) protein is an RNA-binding protein that plays a critical role in various cellular processes, including RNA metabolism, gene regulation, and stress response. Its involvement in neurodegenerative diseases, particularly amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), has drawn significant research interest. Mutations in the FUS gene can lead to its mislocalization and aggregation in the cytoplasm, contributing to the pathogenesis of these disorders. The understanding of FUS functions and its pathogenic variants is vital for developing potential therapeutic strategies. Research has focused on elucidating the molecular mechanisms underlying FUS's role in the nucleus, its interaction with RNA, and the implications of its dysregulation in disease. Moreover, FUS is being studied as a model for exploring general principles of protein misfolding and aggregation relevant to a wide range of neurodegenerative conditions. As such, FUS recombinant proteins have become essential tools for studying its functional properties, investigating RNA interactions, and assessing potential molecular interventions that could mitigate the effects of FUS-associated diseases.
