Analytical Data
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Gene name
U2AF1
- Application
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Alternative Names
U2AF1；U2AF35；Splicing factor U2AF 35 kDa subunit
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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
Q01081-2
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Expression Region
1-240aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAEYLAS IFGTEKDKVN CSFYFKIGAC RHGDRCSRLH NKPTFSQTIL IQNIYRNPQN SAQTADGSHC AVSDVEMQEH YDEFFEEVFT EMEEKYGEVE EMNVCDNLGD HLVGNVYVKF RREEDAEKAV IDLNNRWFNG QPIHAELSPV TDFREACCRQ YEMGECTRGG FCNFMHLKPI SRELRRELYG RRRKKHRSRS RSRERRSRSR DRGRGGGGGG GGGGGGRERD RRRSRDRERS GRF
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Molecular Weight
30 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 critical component of the spliceosome, plays a pivotal role in pre-mRNA splicing by recognizing the polypyrimidine tract in introns, thus facilitating the recruitment of additional splicing factors. Mutations in the U2AF1 gene have been linked to various hematological malignancies, including myelodysplastic syndromes and acute myeloid leukemia, making it a significant focus of cancer research. The heterozygous mutations often occur at residues 34 and 57, leading to abnormal splicing events and the production of aberrant transcripts that contribute to tumorigenesis. Research on U2AF1 has expanded to investigate its structural and functional dynamics, including the implications of these mutations on splice site selection and the subsequent impact on gene expression. Understanding the mechanisms by which U2AF1 mutations disrupt normal splicing processes is crucial for developing targeted therapeutic strategies. Recombinant U2AF1 protein studies enable comprehensive functional assays and structural analyses, providing insights into the altered splicing landscape in cancer. Through these investigations, researchers aim to elucidate the molecular underpinnings of splicing dysregulation in tumors, paving the way for novel diagnostic and therapeutic approaches aimed at mitigating the effects of U2AF1-associated malignancies.
