Recombinant Human DNA- (APEX1) Protein (His)

Name: Recombinant Human DNA- (APEX1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08628P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human DNA- (APEX1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P27695
Target Symbol	APEX1
Synonyms	AP endonuclease 1; AP endonuclease class I; AP lyase; APE 1; APE; APE-1; APEN; APEX 1; APEX; APEX nuclease (multifunctional DNA repair enzyme) 1; Apex nuclease 1; APEX nuclease; APEX1; APEX1_HUMAN; Apurinic endonuclease; Apurinic-apyrimidinic endonuclease 1; Apurinic/apyrimidinic (abasic) endonuclease; Apurinic/apyrimidinic endonuclease 1; Apurinic/apyrimidinic exonuclease; APX; BAP1; Deoxyribonuclease (apurinic or apyrimidinic); DNA (apurinic or apyrimidinic site) lyase; DNA-(apurinic or apyrimidinic site) lyase; mitochondrial; EC 4.2.99.18; HAP 1; HAP1; Human Apurinic endonuclease 1; MGC139790; Multifunctional DNA repair enzyme; Redox factor 1; Redox factor-1; REF 1; REF 1 protein; REF-1; REF1; REF1 protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	KNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL
Expression Range	32-318aa
Protein Length	Full Length of Mature Protein
Mol. Weight	36.2kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are 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.
Subcellular Location	Nucleus. Nucleus, nucleolus. Nucleus speckle. Endoplasmic reticulum. Cytoplasm.; [DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]: Mitochondrion.
Protein Families	DNA repair enzymes AP/ExoA family
Database References	HGNC: 587 OMIM: 107748 KEGG: hsa:328 STRING: 9606.ENSP00000216714 UniGene: PMID: 28882023 The redox domain of APE1 is necessary for the active mode of stimulation of DNA glycosylases (OGG1, MPG, MBD4). APE1-catalyzed oligomerization along DNA induces helix distortions, which in turn enable conformational selection and stimulation of DNA glycosylases. PMID: 29475157 APE1 removes 3' mismatches and DNA damage by placing the 3' group within the intra-helical DNA cavity via a non-base flipping mechanism. PMID: 29374164 This study identified 2837 genes whose expression is significantly changed following APE1 knockdown in pancreatic ductal adenocarcinoma. PMID: 28922540 MCP- and CP-induced oxidative stress alters APE1-dependent BER-pathway and also mediates cell survival signalling mechanisms via APE1 regulation, thereby promoting lung cancer cell survival and proliferation. PMID: 28887667 Study uncovered a novel interaction between APE1 and PRDX1, which existed in both the nuclear and cytosolic fractions. The loss of APE1 interaction with PRDX1 promotes APE1 redox function to activate binding of the transcription factor NF-kappaB onto the promoter of IL-8 involved in cancer invasion and metastasis, resulting in its upregulation. PMID: 27388124 APE1 contributes to the protective effects of resveratrol against neonatal hypoxicischemic brain injuries, and suggest that DNA repair enzymes, including APE1, may be a unique strategy for neuroprotection against this disease. PMID: 29039534 Studied the association between single-nucleotide polymorphism of apurinic/apyrimidinic endonuclease 1 (APEX1) rs1760944 and risk of nasopharyngeal carcinoma in a Chinese population. PMID: 28464393 this study demonstrates a novel role of extracellular APE1 in IL-6-dependent cellular responses. PMID: 28751279 Our results showed that DNA base excision repair proteins APE-1 and XRCC-1 are overexpressed in tongue squamous cell carcinoma and that XRCC-1 is associated with better clinical staging and nodal status. PMID: 27925687 For the first time, this work identifies Ref-1 as a novel molecular effector in T-ALL and demonstrates that Ref-1 redox inhibition results in potent inhibition of leukemia T cells, including relapsed T-ALL. These data also support E3330 as a specific Ref-1 small-molecule inhibitor for leukemia PMID: 28446640 Apurinic/apyrimidinic endonuclease 1 is downregulated in Pleomorphic Adenomas of salivary gland and overexpressed in Carcinoma ex Pleomorphic Adenomas, the increased expression of this protein is associated with a more aggressive behavior in Carcinoma ex Pleomorphic Adenomas, which suggests that this protein may represent a prognostic biomarker in the studied Salivary Gland Tumors. PMID: 28523411 our study demonstrates that elevation of acetylation level of APE1 in tumor could be a novel mechanism by which cells handle the elevated levels of DNA damages in response to genotoxic stress and maintain sustained proliferation. PMID: 27655688 The chemotherapy-naive serum APE1 level, which correlated with its tissue level inversely associated with progression-free survival of platinum-containing doublet chemotherapy, whereas post-treatment serum APE1 level was inversely associated with overall survival. PMID: 27813497 HOGG1 Ser326Cys, APE1 Asp148Glu and XRCC1 Arg399Gln polymorphisms are correlated with the risk and clinicopathological features of PACG. PMID: 28396513 Through the characterization of the interactomes of APE1 with RNA and other proteins, we demonstrate here a role for APE1 in pri-miRNA processing and stability via association with the DROSHA-processing complex during genotoxic stress. We also show that endonuclease activity of APE1 is required for the processing of miR-221/222 in regulating expression of the tumor suppressor PTEN. PMID: 28986522 the APEX1 Asp148Glu polymorphism might be important in stimulating the development of prostate cancer rather than its invasiveness in various populations, especially for Asians. PMID: 27248666 our data reinforce the concept that non-synonymous APE1 variants present in the human population may act as cancer susceptibility alleles PMID: 27050370 Data suggest that APE1 could be a potential target for NSCLC metastasis and AT101 is a potent inhibitor in further treatment of NSCLC patients. PMID: 27074577 Our findings suggest that constitutive overexpression of APE1 in esophageal adenocarcinoma may be an adaptive pro-survival mechanism that protects against the genotoxic lethal effects of bile reflux episodes. PMID: 26934647 our study demonstrates that increased acetylation levels of APE1 in tumor cells inhibit the limited N-terminal proteolysis of APE1 and thereby maintain the functions of APE1 to promote tumor cells' sustained proliferation and survival. PMID: 26981776 Data indicate that apurinic/apyrimidinic endonuclease-1 (APE1) efficiently process an abasic ribonucleoside 5'-monophosphates (rNMPs) site in DNA and have weak endoribonuclease and 3'-exonuclease activities on r8oxoG substrate. PMID: 28977421 These results suggested that the expression of APE1 was an important basis for the maintenance of poly (ADP-ribose) polymerase 1, and the deletion of APE1 may be related to the resistance of triple-negative breast cancer to olaparib. PMID: 29064327 Alleles in mitochondrial transcription factor A (TFAM) and AP endonuclease 1 (APE1) are associated with reduced cognitive performance. PMID: 28242328 Study shows that TRX1 and APEX1 expressions are up regulated in new Multiple Sclerosis (MS) patients compared to controls and might be implicated in pathogenesis of the disease. PMID: 28844667 Ku antigen displays the AP lyase activity on a certain type of double-stranded DNA. PMID: 27129632 study demonstrates that APE1 overexpression is an independent prognostic marker, but exclusively in ERG-negative prostate cancers PMID: 28467610 These results suggest that degradation of endogenous APE1 by Parkin occur when cells are stressed to activate Parkin, and imply a role of Parkin in maintaining the quality of APE1, and loss of Parkin may contribute to elevated APE1 levels in glioblastoma. PMID: 27148961 The efficiency of AP site cleavage by APE1 was affected by the benzo[a]pyrenyl-DNA adduct (BPDE-dG) in the opposite strand. PMID: 28065385 Enforced expression of hOGG1 and hAPE significantly protected thalamic neurons and motor neurons from retrograde apoptosis induced by target deprivation and axotomy. PMID: 27364693 This study supported the hypothesis that the APE1 rs1760944 T>G polymorphism may be associated with N,N-dimethylformamide -induced abnormal liver function in the Chinese Han population. PMID: 27463724 Repair of the uracil adjacent to cisplatin ICLs proceeds through the classical BER pathway, highlighting the importance of specific proteins in this redundant pathway. Removal of uracil is followed by the generation of an abasic site and subsequent cleavage by AP endonuclease 1 (APE1). Inhibition of either the repair or redox domain of APE1 gives rise to cisplatin resistance. PMID: 28110804 Overexpressed APE1 promotes ovarian cancer growth and metastasis. Downregulated APE1 could suppress cell activity via AP-1 pathway, suggesting that APE1 gene may be a potential therapeutic target for ovarian cancer. PMID: 27553367 Our results indicate that the tumor-associated APE1 R237C variant is a possible susceptibility factor, but not likely a driver of cancer cell phenotypes. PMID: 28181292 Association of the APE1 single nucleotide polymorphism rs3136820 and the levels of abasic sites in human leukocytes derived from breast cancer patients PMID: 27539671 APE1 acetylation is an integral part of the base excision repair pathway for maintaining genomic integrity. PMID: 27994014 Effects of monovalent (K(+)) and divalent (Mg(2+), Mn(2+), Ca(2+), Zn(2+), Cu(2+), and Ni(2+)) metal ions on DNA binding and catalytic stages of APEX1 were studied. PMID: 27063150 Individuals with the variant TG genotypes had a significantly increased risk of female infertility. Whereas, a significant association between 1349T > G polymorphism and female infertility risk was not observed. PMID: 26790616 APE1 Accelerates turnover of OGG1 by preventing retrograde binding to the abasic-site product. PMID: 28345889 The results demonstrate a crucial role of APE1 3' to 5' exonuclease activity in combating mutations in CpG clusters caused by an intermediate of DNA demethylation during base excision repair. PMID: 27183823 In an in vivo model of restenosis, which is characterized by oxidative stress, endothelial activation, and smooth muscle cell proliferation, Thioredoxin-1 protein levels are reduced in the endothelium of the carotids. APEX1 acts anti-apoptotic in endothelial cells. This anti-apoptotic effect depends on the first 20 amino acids of APEX1 PMID: 27835927 While DNA conformational alteration is negligible, APE1 enzyme shows characteristic changes in the alpha helix and beta strand ratio after incubation with G. lucidum extract. The enhanced reactivity of APE1 at the molecular level in the presence of G. lucidium is attributed to this effect. PMID: 27240987 These results strongly indicate that anti-inflammatory effects in TNF-alpha-stimulated endothelial cells by acetylation are tightly linked to secreted APE1/Ref-1, which inhibits TNF-alpha binding to TNFR1 by reductive conformational change, with suggestion as an endogenous inhibitor of vascular inflammation. PMID: 26964514 Polymorphism in XRCC1 and APE1 gene is associated with an increased risk of COPD. PMID: 27107596 Data indicate conserved amino acid residues in the nucleotide incision repair (NIR)-specific enzymes of human APE1 and Bacillus subtilis ExoA.. PMID: 27343627 Based on these results, we conclude that the APEX gene polymorphism Ile64Val may be associated with an increased risk of colorectal cancer. PMID: 26146106 Serum levels of APE1/Ref-1 in bladder cancer patients were significantly elevated compared to those of the control group. Serum APE1/Ref-1 levels are associated with tumor stage, grade, muscle invasion, and recurrence. PMID: 25672588 OGG1 and APE1 polymorphisms are associated with stage- and sex-specific risk of colorectal carcinoma in the Taiwanese population. PMID: 27022219 Our study suggested that the APE1 protein is important for the proliferation and growth of ovarian cancer cells. APE1 silencing might enhance drug-sensitivity, and thus APE1 might serve as a novel anti-OC therapeutic target. PMID: 27802207 Our study identified that the APE1 -656 T>G polymorphism may contribute to the susceptibility of noise-induced hearing loss. PMID: 26507517

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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Recombinant Human DNA- (APEX1) Protein (His)

Recombinant Human DNA- (APEX1) Protein (His)

Product Overview

Target Details

FAQs