Analytical Data
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Gene name
DDB2
- Application
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Alternative Names
DDB2；DNA damage-binding Protein 2
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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
Q92466
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Expression Region
1-427aa
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AA Sequence
MAPKKRPETQKTSEIVLRPRNKRSRSPLELEPEAKKLCAKGSGPSRRCDSDCLWVGLAGPQILPPCRSIVRTLHQHKLGRASWPSVQQGLQQSFLHTLDSYRILQKAAPFDRRATSLAWHPTHPSTVAVGSKGGDIMLWNFGIKDKPTFIKGIGAGGSITGLKFNPLNTNQFYASSMEGTTRLQDFKGNILRVFASSDTINIWFCSLDVSASSRMVVTGDNVGNVILLNMDGKELWNLRMHKKKVTHVALNPCCDWFLATASVDQTVKIWDLRQVRGKASFLYSLPHRHPVNAACFSPDGARLLTTDQKSEIRVYSASQWDCPLGLIPHPHRHFQHLTPIKAAWHPRYNLIVVGRYPDPNFKSCTPYELRTIDVFDGNSGKMMCQLYDPESSGISSLNEFNPMGDTLASAMGYHILIWSQEEARTRK
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Molecular Weight
53.8 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
DDB2, or damage-specific DNA binding protein 2, plays a crucial role in the nucleotide excision repair (NER) pathway, which is essential for repairing DNA damage caused by ultraviolet (UV) light and other mutagenic agents. As a key component of the damage recognition complex, DDB2 binds to damaged DNA sites, facilitating the recruitment of other proteins involved in the repair process. Research into DDB2 recombinant proteins has gained momentum due to their potential applications in understanding cancer biology, as defects in NER can lead to increased susceptibility to skin cancers and other malignancies. Additionally, recombinant DDB2 proteins serve as valuable tools for investigating the mechanics of DNA repair, evaluating therapeutic strategies, and developing potential biomarkers for cancer diagnostics. The ability to produce DDB2 in a laboratory setting allows researchers to explore its structural properties, binding affinities, and interactions with other proteins. Understanding these aspects can provide insights into how cells maintain genomic integrity and respond to DNA damage, fostering advancements in both basic and applied biomedical research. Overall, the study of DDB2 and its recombinant forms holds significant promise for enhancing our comprehension of DNA repair mechanisms and their implications in human health.
