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-His;N-MBP
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35637-1
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Expression Region
M1-Y526
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Molecular Weight
95 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 implicated in various cellular processes, such as RNA processing, transport, and regulation of gene expression. Originally identified as a fusion partner in certain cancers, its role has expanded into neurobiology, especially concerning neurodegenerative diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). The aggregation of FUS in the cytoplasm is a hallmark of these diseases, suggesting that dysregulation of protein homeostasis may contribute to neuronal degeneration. Given its critical involvement in RNA metabolism and its association with pathological conditions, FUS has become an important target for research aimed at understanding the molecular mechanisms of these diseases. Furthermore, the development of FUS recombinant proteins for biochemical studies allows scientists to investigate its functional properties and interactions with RNA and other proteins, shedding light on the mechanisms underlying its aggregation and toxicity in neuronal cells. This research is not only pivotal for elucidating the pathogenesis of neurodegenerative disorders but also holds potential for therapeutic advancements, making FUS an essential focus in both cancer and neurobiology research.
