Recombinant Human Endonuclease 8-Like 1 (NEIL1) Protein (His-SUMO)

Name: Recombinant Human Endonuclease 8-Like 1 (NEIL1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09915P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Endonuclease 8-Like 1 (NEIL1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q96FI4
Target Symbol	NEIL1
Synonyms	DNA (apurinic or apyrimidinic site) lyase Neil1; DNA glycosylase/AP lyase Neil 1; DNA glycosylase/AP lyase Neil1; DNA-(apurinic or apyrimidinic site) lyase Neil1; Endonuclease 8 like 1; Endonuclease 8-like 1; Endonuclease VIII; Endonuclease VIII like 1; Endonuclease VIII-like 1; FLJ22402; FPG1; hFPG1; NEH 1; NEH1; NEI 1; Nei endonuclease VIII like 1 (E. coli); Nei endonuclease VIII like 1; Nei homolog 1; Nei like 1; Nei like protein 1; Nei-like protein 1; NEI1; NEIL 1; Neil1; NEIL1_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	PEGPELHLASQFVNEACRALVFGGCVEKSSVSRNPEVPFESSAYRISASARGKELRLILSPLPGAQPQQEPLALVFRFGMSGSFQLVPREELPRHAHLRFYTAPPGPRLALCFVDIRRFGRWDLGGKWQPGRGPCVLQEYQQFRENVLRNLADKAFDRPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARSVLEALQQHRPSPELTLSQKIRTKLQNPDLLELCHSVPKEVVQLGGKGYGSESGEEDFAAFRAWLRCYGMPGMSSLQDRHGRTIWFQGDPGPLAPKGRKSRKKKSKATQLSPEDRVEDALPPSKAPSRTRRAKRDLPKRTATQRPEGTSLQQDPEAPTVPKKGRRKGRQAASGHCRPRKVKADIPSLEPEGTSAS
Expression Range	2-390aa
Protein Length	Full Length of Mature Protein
Mol. Weight	59.6kDa
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	Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.
Subcellular Location	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Chromosome. Note=During mitosis, associates with centrosomes and condensed chromatin.
Protein Families	FPG family
Database References	HGNC: 18448 OMIM: 608844 KEGG: hsa:79661 STRING: 9606.ENSP00000347170 UniGene: PMID: 29522991 The major role of acetylable Lys residues in NEIL1 is to stabilize the formation of chromatin-bound repair complexes which protect cells from oxidative stress. PMID: 29698889 The level of OGG1 expression was significantly reduced in bipolar patients compared to healthy individuals, whereas the two groups exhibited similar levels of NEIL1 expression. PMID: 29626765 identified the c-Jun N-terminal kinase 1 (JNK1) as the kinase involved in the phosphorylation of NEIL1 PMID: 27518429 NEIL1 (rs5745908) is associated with Behcet's disease. The genetic association in NEIL1 is a predicted splice donor variant that may introduce a deleterious intron retention and result in a noncoding transcript variant. PMID: 26662719 cellular NEIL1 is regulated by the UPP mediated by the E3 ubiquitin ligases Mule and TRIM26, which plays a vital role in co-ordinating the cellular response to DNA damage. PMID: 27924031 Nei Like DNA Glycosylase 1 (NEIL1) as a likely candidate gene due to its crucial role in B-cell activation and terminal differentiation. PMID: 28093361 NEIL1 and NEIL2 cooperate with TDG during base excision: TDG occupies the abasic site and is displaced by NEILs, which further process the baseless sugar, thereby stimulating TDG-substrate turnover. PMID: 26751644 first study to show that SNPs of genes involved in DNA repair, may modulate the risk of Depressive Disorder. PMID: 26074017 Findings suggesting that DNA glycosylase NEIL1 c.C844T is a defective allele. PMID: 26095805 NEIL1 forms a multiprotein complex with DNA replication proteins via its C-terminal domain, allowing recruitment at the replication fork. PMID: 26134572 Results show that YB-1 interferes negatively with the AP site DNA cleavage activity of both APE1 and NEIL1 for ssDNA and bubble structures. PMID: 25605055 Rad9 regulates base excision repair by controlling NEIL1 transcription. PMID: 25873625 genome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase PMID: 24382305 The NEIL1 rs4462560 SNP may serve as a predictor of acute RIET and RP risk but not of overall survival. PMID: 24022861 Prereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins. PMID: 23898192 Authors show that the intrinsically disordered C-terminal domain interacts with the folded domain in native NEIL1 containing 389 residues. PMID: 23542007 NEIL1 recognizes specifically and distinctly interstrand crosslinks in DNA, and can obstruct the efficient removal of lethal crosslink adducts. PMID: 23508956 binds to the BRCT domain of PARP-1 PMID: 23104860 aberrant promoter methylation of NEIL1 in head and neck squamous cell carcinoma PMID: 22286769 NEIL1 gene mutation may have a causative role in the development of type 2 diabetes in the Turkish population. PMID: 21985917 we demonstrated that hNEIL1 and hNTH1 cleave Oz sites as efficiently as 5-hydroxyuracil sites. Thus, hNEIL1 and hNTH1 can repair Oz lesions PMID: 22465744 the hnRNP-U protection of cells after oxidative stress is largely due to enhancement of NEIL1-mediated repair. PMID: 22902625 Pro2 and Lys54 are involved in the AP lyase activity; Met81, Arg119 and Phe120 are essential for removal of 8-oxoG in duplex DNA PMID: 22858590 the binding of these modified DNAs with the unedited and edited forms of human NEIL1 along with E. coli Endo III PMID: 22639086 Structural characterization of viral ortholog of human DNA glycosylase NEIL1 bound to thymine glycol or 5-hydroxyuracil-containing DNA. PMID: 22170059 Homozygosity mapping and exome sequencing in a consanguineous kindred identified MYO1E and NEIL1 as novel candidate genes for human autosomal recessive steroid-resistant nephrotic syndrome. PMID: 21697813 These data suggest Neil1 may be a critical mediator of base excision repair of incorporated dUMP following thymidylate synthetase pathway inhibition. PMID: 21131780 enzymological activity in peripheral leukocytes is increased in children with asthma bronchiale PMID: 19840299 NEIL1 recoding site is a preferred editing site for the RNA editing adenosine deaminase ADAR1. PMID: 21068368 WRN is the only human RecQ helicase that stimulates NEIL1 DNA glycosylase activity, and that this stimulation requires a double-stranded DNA substrate. PMID: 20346739 Modulation of NEIL1's activity on single-stranded DNA substrate by RPA and PCNA support NEIL1's involvement in repairing the replicating genome. PMID: 20338831 These results suggest that, in vivo, NEIL1 functions either at nucleosome-free regions (such as those near replication forks) or with cofactors that limit its non-specific binding to DNA. PMID: 20005182 The results indicate that NEIL1 does not require a base opposite to identify and remove hydantoin lesions. PMID: 20099873 Pyrimidine dimer repair enzyme located on the long arm of chromosome 15 that is frequently deleted in human cancers. PMID: 12509226 NEIL1 and NEIL2 are preferentially involved in repair of lesions in DNA bubbles generated during transcription and/or replication PMID: 14522990 hNEIL1 has a significant role in the repair of 5S-Tg in human cells. PMID: 14734554 Overproduction, crystallization and preliminary crystallographic analysis of NEIL1 PMID: 15159582 zincless finger appears to be required for NEIL1 activity, because mutating a very highly conserved arginine within this motif greatly reduces the glycosylase activity of the enzyme. PMID: 15232006 Reduced expression of NEIL1 is associated with the pathogenesis of gastric cancers PMID: 15319300 NEIL1 and OGG1, two DNA glycosylases which do not stably interact with each other, stimulate 8-oxoguanine repair by a collaboration that is possible because of higher abasic (AP) site affinity and stronger AP lyase activity of NEIL1 relative to OGG1. PMID: 15350146 NEIL1 is a DNA glycosylase that excise 5-formyluracil, 5-hydroxymethyluracil and Thymine glycol in human cells. PMID: 15533839 Oxidative stress-induced activation of NEIL1 appears to be involved in the feedback regulation of cellular repair activity needed to handle an increase in the level of oxidative base damage PMID: 16118226 Nth1 released 5R,6S 2'-deoxyribonucleoside diastereoisomer (Tg2) much more rapidly than cis 5S,6R-deoxyribonucleoside diastereoisomer (Tg1) regardless of the opposing purine. Neil1 released Thymine glycol non-stereoselectively. PMID: 16446124 A T434+2C mutation was found in familial colorectal cancer DNA suggesting a limited role for this gene in the devlopment of CRC. PMID: 17029639 The damage specificity of human homologues of Endo III (hNTHl) and Endo VIII (hNEIL1 and hNEIL2) is compared to elucidate the repair role in cells. PMID: 17150535 we found that although both SMUG1 and NEIL1 are able to excise 5-OHU lesions located in the proximity of the proximity of the 3'-end of a DNA SSB, NEIL1 is more efficient in the repair of these DNA lesions. PMID: 17348689 Human NEIL1 DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately and by the 9-1-1 complex. PMID: 17395641 The ability of Neil1 to recognize a variety of pyrimidine lesions is connected to the flexible binding pocket of the enzyme and the common chemical features of lesions that contain a pyrimidine ring. PMID: 17432829 Centrosomal localization of hNEIL1 was observed when mitotic HeLa cells were immunostained with hNEIL1 antibodies PMID: 17556049

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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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