Analytical Data
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Gene name
DFFA
- Application
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Alternative Names
DFFA；DFF1；DFF45;DNA fragmentation factor subunit alpha
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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
O00273
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Expression Region
1-331aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMEVTGDAGVPESGEIRTLKPCLLRRNYSRE QHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLP SNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQ LKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLD QREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRE TSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIK KTETVQEACEWELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDP T
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Molecular Weight
39 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
DFFA, or Death-Domain-Associated Protein, is an important protein in the study of apoptosis and cellular signaling. The DFFA gene encodes a protein that plays a critical role in programmed cell death, a fundamental process for maintaining cellular homeostasis and development. Research has shown that DFFA interacts with various cellular pathways and proteins, influencing the apoptotic signaling cascade. Understanding the structure and function of DFFA is crucial for elucidating its role in different biological processes, including cancer progression, neurodegenerative diseases, and immune responses. Recent advancements in biotechnology and recombinant protein expression systems have enabled researchers to produce and study DFFA in its purified form, which facilitates investigations into its molecular mechanisms. By exploring DFFA's interactions and post-translational modifications, scientists hope to uncover potential therapeutic targets for modulating apoptosis in diseases where this process is disrupted. Additionally, studying DFFA's role in various physiological and pathological contexts may reveal insights into its involvement in tumorigenesis and other diseases, paving the way for novel strategies in targeted therapies. Through continued research, DFFA is becoming increasingly recognized as a pivotal player in the regulation of cell death and survival, making it a significant focus of cellular biology and biomedicine.
