Analytical Data
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Gene name
polB
- Application
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Alternative Names
(Pol II)
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21189
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Expression Region
2-783aa
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Molecular Weight
97.4 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
Related Products
Protein Description
Polymerase beta (polB) is a crucial enzyme involved in DNA repair and replication processes, playing a significant role in maintaining genomic stability. Researchers have been interested in polB due to its implications in various biological processes, including cell survival following DNA damage, where its activity can influence the outcome of mutagenesis and carcinogenesis. The enzyme exhibits a unique ability to incorporate nucleotides opposite damaged bases, making it essential for the base excision repair pathway. The study of polB has been further stimulated by its potential as a therapeutic target; alterations in its function are often associated with an increased risk of cancer, particularly in cases of colorectal and breast tumors. Recent advances in recombinant protein expression techniques have enabled the detailed characterization of polB's structure and function, including its catalytic mechanisms and interactions with other repair proteins. Understanding the nuances of polB's role in DNA metabolism can provide insights into new strategies for cancer treatment and improve our knowledge of DNA repair pathways, which is crucial for developing effective therapies against malignancies characterized by defective repair mechanisms. Consequently, ongoing research into polB not only highlights its fundamental biological significance but also underscores its potential as a promising target for therapeutic intervention in cancer and other diseases associated with DNA damage.
