Recombinant Human DNA- (apurinic or apyrimidinic site) lyase (APEX1)

SKU:BHP10502196
Overview
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Recombinant APEX1 Human protein produced in Yeast (S. cerevisiae), N-terminal 6xHis-tagged spanning 32-318aa. Suitable for binding assays, functional studies, and assay development.
Expression System Yeast (S. cerevisiae)
Tag N-terminal 6xHis-tagged
Purity Greater
Species Human
Molecular Weight 34.2 kDa
Options selector
Catalog no. Size
CSB-YP001900HU-1MG 1 mg
CSB-YP001900HU-100UG 100 ug
CSB-YP001900HU-20UG 20 ug
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) - 1 mg, 100 ug, 20 ug
  • Lead time: In Stock at Manufacturer. Lead time is typically 3-7 business days.
  • Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No CSB-YP001900HU
Activity
  • Not Test
Alternative Names APEX nuclease ;APENApurinic-apyrimidinic endonuclease 1 ;AP endonuclease 1 ;APE-1REF-1Redox factor-1
Endotoxin Level Not test
Expression System
  • Yeast (S. cerevisiae)
Form Liquid or Lyophilized powder
Function
  • Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage
  • generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids
  • single-stranded DNA regions of R-loop structures
  • and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand
  • APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain
  • such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6
  • associates with nCaRE
  • acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity
  • when acetylated at Lys-6 and Lys-7
  • leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1
  • plays a role in the rRNA quality control process during cell cycle progression. Associates
  • together with YBX1
  • on the MDR1 promoter. Together with NPM1
  • associates with rRNA. Binds DNA and RNA.
Molecular Weight 34.2 kDa
Product Type
  • Recombinant Protein
Purity Greater than 90% as determined by SDS-PAGE.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Species Homo sapiens (Human)
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
UniProt # P27695

Scientific Background

Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents.

Product Description

Yeast (S. cerevisiae) Expression

Recombinant Human DNA- (apurinic or apyrimidinic site) lyase (APEX1) is a recombinant protein expressed in Yeast (S. cerevisiae) and purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. Supplied as Liquid or Lyophilized powder, n-terminal 6xhis-tagged. For research use only.

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Specifications

Molecular Weight 34.2 kDa
Expression Region 32-318aa
Expression System Yeast (S. cerevisiae)
Tag N-terminal 6xHis-tagged
Purity Greater than 90% as determined by SDS-PAGE.
Form Liquid or Lyophilized powder
Storage Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Endotoxin Level Not test
UniProt Accession P27695
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Safety & Handling

For Research Use Only (RUO). Not intended for diagnostic or therapeutic use. Handle as potentially biohazardous material. Follow your institution's biosafety guidelines when working with recombinant proteins.

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What expression system was used to produce this protein?

This recombinant protein is expressed in Yeast (S. cerevisiae), a widely used system for producing soluble, biologically active proteins at scale. The Yeast (S. cerevisiae) expression platform enables efficient folding and high yields, suitable for functional and binding assays.

What is the tag and purity of this product?

This protein is supplied as N-terminal 6xHis-tagged and has been purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. High purity minimizes interference in downstream assays, particularly in cell-based bioactivity studies and ELISA development.

How should I reconstitute and store this product?

Briefly centrifuge the vial before opening. Reconstitute in sterile deionized water to 0.1–1.0 mg/mL. For long-term storage, add 5–50% glycerol and store in aliquots at -20°C or -80°C to avoid repeated freeze-thaw cycles. The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Is this protein biologically active?

Biological activity data are available in the product datasheet. Please contact our support team for activity specifications relevant to your specific application.

What applications is this recombinant protein suitable for?

This recombinant protein is suitable for a range of in vitro research applications including binding assays, protein–protein interaction studies, cell proliferation/bioactivity assays, ELISA standard curve calibration, and assay development. Confirm suitability for your specific assay conditions with the product datasheet.

We offer flexible ordering options including bulk quantities, custom formulations, and endotoxin removal services for many of our recombinant proteins. Lead times and minimum order quantities vary by product. For custom conjugation, specialized buffer formulations, or volume pricing, please contact our support team. All customization requests are handled in partnership with our manufacturing suppliers and are subject to feasibility review.

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