Analytical Data
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Gene name
APE3
- Application
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Alternative Names
APE3; YBR286W; YBR2024Aminopeptidase Y; EC 3.4.11.15
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Species
Saccharomyces cerevisiae
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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
P37302
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Expression Region
57-537aa
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Molecular Weight
58.9 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
APE3 (AP Endonuclease 3) is a crucial enzyme involved in the base excision repair (BER) pathway, which is responsible for repairing DNA lesions caused by oxidative stress, environmental damage, and normal cellular processes. As a member of the AP endonuclease family, APE3 plays a vital role in correcting single-strand breaks and removing damaged nucleotides, thus maintaining genomic integrity. Its importance in cellular responses to DNA damage has sparked considerable research interest, particularly regarding its potential implications in cancer and other diseases characterized by genomic instability. Studies have shown that APE3 exhibits unique properties compared to other members of the AP endonuclease family, such as a broader substrate specificity and distinct enzymatic mechanisms. Understanding the structure and function of APE3, as well as the regulation of its activity, can provide insights into its role in therapeutic resistance and disease progression. Furthermore, the recombinant protein expression of APE3 offers opportunities for detailed biochemical characterization and the exploration of its potential as a drug target. Given the growing body of evidence linking APE3 to various pathological conditions, including its aberrant expression in tumors, research in this area has the potential to yield novel strategies for cancer treatment by targeting the enzyme's activity to enhance the effectiveness of existing therapies or to develop new pharmacological agents.
