Analytical Data
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Gene name
AF1Q
- Application
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Alternative Names
AF1Q; AF1Q_HUMAN; ALL1 fused gene from chromosome 1q; MLLT 11; MLLT11
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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
Q13015
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Expression Region
1-90aa
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AA Sequence
MRDPVSSQYS SFLFWRMPIP ELDLSELEGL GLSDTATYKV KDSSVGKMIG QATAADQEKN PEGDGLLEYS TFNFWRAPIA SIHSFELDLL
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Molecular Weight
10 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
AF1Q, a protein encoded by the AF1Q gene, plays a significant role in various cellular processes, particularly in the context of cancer research and cellular differentiation. This protein is known to be involved in regulating transcription and interacting with various transcription factors, suggesting its potential influence on gene expression and cellular behavior. Recent studies have highlighted AF1Q's involvement in the pathogenesis of several malignancies, including leukemia and solid tumors, where it may contribute to oncogenic pathways. The interest in AF1Q also stems from its structural features, which include a unique domain that facilitates interactions with other proteins, making it a candidate for further exploration in therapeutics. Researchers are employing recombinant DNA technology to produce AF1Q as a fusion protein, allowing for better characterization of its functional properties and interactions. By systematically investigating AF1Q through techniques such as Western blotting, immunoprecipitation, and functional assays, scientists aim to elucidate its role in cellular signaling networks. Understanding the molecular mechanisms involving AF1Q could pave the way for innovative strategies in targeted therapies, particularly for cancers where its expression is deregulated.
