Analytical Data
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Gene name
U2AF1
- Application
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Alternative Names
U2 auxiliary factor 35KDA subunit U2 small nuclear RNA auxiliary factor 1 U2 snRNP auxiliary factor small subunit
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q01081
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Expression Region
1-240aa
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Molecular Weight
54.9 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
U2AF1, a vital component of the spliceosome, plays a critical role in pre-mRNA splicing by recruiting spliceosomal machinery to intron-exon junctions. Mutations in the U2AF1 gene have been implicated in various hematological malignancies, including myelodysplastic syndromes and acute myeloid leukemia. These mutations often impact the protein's ability to recognize splice sites, leading to aberrant splicing and the production of dysfunctional proteins that contribute to oncogenesis. Given its significant role in RNA processing and the association of U2AF1 mutations with cancer, researchers are increasingly focused on characterizing the protein’s structure and function. Recombinant U2AF1 proteins have been extensively studied to elucidate the molecular mechanisms of splicing regulation and the effects of disease-associated mutations. Understanding U2AF1's functional dynamics is crucial for developing targeted therapies that can mitigate the consequences of splicing aberrations in cancer. This research not only sheds light on fundamental cellular processes but also holds potential for advancing therapeutic strategies in treating U2AF1-related malignancies.
