Analytical Data
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Gene name
dinB
- Application
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Alternative Names
dinB;DINB1;DNA polymerase kappa
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Species
Colwellia
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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
Q487H6
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Expression Region
1-352aa
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AA Sequence
MGNQKKIIHIDMDCFYAAIEMRDFPEYQNIPLAVGGDGPRSVLCTSNYQARQFGVRSAMPAIKAKQLCPHLKIVHGRMDVYKETSKNIREIFSRYTDLIEPLSLDEAYLDVTDATMCQGSATLIAERIRADIFNELNLTASAGIAPNKFLAKIASDENKPNGQCVITPDKVANFVEQLSLKKIPGIGPKTFEKLNRHGYVTCADVRQSNIRALQNIVGKFANSLYLKSHGVDNRDLEVSRQRKSLAIETTLAHDISTQDECKLVIDSLYQKLLTRLAPHSNREIIRQGVKLKFTDFNQTTVETQSNECQQALFISLLSKAYSRSNKRGVRLVGLTLGFADSPGESQQLSLSL
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Molecular Weight
43.3 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
DinB is a translesion synthesis (TLS) DNA polymerase that plays a crucial role in DNA damage tolerance in prokaryotic organisms, primarily in Escherichia coli. It allows the bypass of DNA lesions that would otherwise stall the replication fork, contributing to the maintenance of genomic integrity under conditions of stress or damage. The study of DinB has garnered significant interest due to its potential implications in understanding bacterial survival mechanisms, antibiotic resistance, and the broader aspects of DNA repair pathways. Research has revealed that DinB can incorporate nucleotides opposite various types of DNA lesions, such as those induced by oxidative stress or alkylation, often with a low fidelity, which can lead to mutations. This mutagenic property is a double-edged sword; while it enables the survival of bacteria under genotoxic stress, it can also promote genetic diversity and adaptability. Moreover, the regulation of DinB expression in response to DNA damage signals further emphasizes its importance in cellular responses to stress. Understanding the structural and functional dynamics of DinB, including its active site, substrate specificity, and interaction with other repair proteins, is essential to unveil the complexity of TLS mechanisms. The ongoing research into DinB's activities and regulatory networks may provide novel insights into bacterial resilience and inform strategies to combat bacterial infections through targeting DNA repair pathways.











