Analytical Data
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Gene name
DNAL4
- Application
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Alternative Names
DNAL4;Dynein axonemal light chain 4
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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
O96015
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Expression Region
1-105aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGETEGKKDEADYKRLQTFPLVRHSDMPEE MRVETMELCVTACEKFSNNNESAAKMIKETMDKKFGSSWHVVIGEGFGFE ITHEVKNLLYLYFGGTLAVCVWKCS
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Molecular Weight
14 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
DNAL4, a member of the DNA ligase family, is primarily studied for its pivotal role in DNA repair and replication processes. The interest in DNAL4 research has surged due to its potential implications in cancer biology and therapeutic applications. It is hypothesized that DNAL4 not only facilitates the joining of DNA ends during repair but also plays a critical role in maintaining genomic stability. Mutations or malfunctions in DNA ligases, including DNAL4, can lead to increased susceptibility to genetic disorders and malignancies, underlining the importance of understanding its mechanism of action. Recent studies have focused on elucidating the structural and functional properties of DNAL4, employing techniques such as X-ray crystallography and cryo-electron microscopy. These investigations aim to reveal the intricacies of its enzymatic function and interactions with other repair proteins. Furthermore, exploring the regulation of DNAL4 expression in various cellular contexts could provide insights into its contribution to tumorigenesis and resistance to therapies. As cancer cells often exploit DNA repair pathways to survive, targeting DNAL4 or its associated pathways may represent a novel approach in cancer treatment. Overall, the research on DNAL4 offers a promising avenue for understanding the complexities of DNA dynamics and holds the potential to aid in the development of innovative cancer therapies.
