Analytical Data
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Gene name
APEX1
- Application
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Alternative Names
APEX1;APE;APE1;APEX;DNA repair nuclease/redox regulator APEX1
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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
P27695
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Expression Region
1-318aa
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AA Sequence
MASMTGGQQMGRGSMPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKE AAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKE EAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSR QCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQ RWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQE RQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFL LSHSLLPALCDSKIRSKALGSDHCPITLYLAL
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Molecular Weight
37 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
APEX1 (apurinic/apyrimidinic endonuclease 1) is a crucial enzyme involved in the base excision repair pathway, which is essential for maintaining genomic stability by repairing DNA damage. The importance of APEX1 in cellular processes has garnered significant attention in the fields of molecular biology and cancer research. It plays a dual role as both a DNA repair protein and a redox regulator, influencing various cellular functions, including transcription regulation and response to oxidative stress. Dysregulation of APEX1 has been linked to several diseases, notably cancer, where its overexpression can contribute to tumorigenesis by facilitating the survival of cells with damaged DNA. Consequently, understanding the structural and functional properties of APEX1 has become a focal point for researchers aiming to elucidate its role in cancer biology and other disorders. Recent advancements in recombinant protein technology have paved the way for the production and characterization of APEX1, enabling detailed studies of its enzymatic mechanisms, interaction with other proteins, and the development of potential therapeutic inhibitors. These investigations are crucial not only for understanding the fundamental biology of DNA repair but also for identifying novel targets for cancer treatment and enhancing the effectiveness of existing therapies.











