NEIL1 Protein, Human (His)

NEIL1 is a critical base excision repair enzyme that recognizes and eliminates damaged bases and preferentially selects oxidized pyrimidines such as thymine glycol, Fapy, and 5-hydroxyuracil. Although NEIL1 has limited activity toward 8-oxoguanine, it has excellent AP lyase activity and introduces nicking by eliminating β-δ. NEIL1 Protein, Human (His) is the recombinant human-derived NEIL1 protein, expressed by E. coli , with C-His labeled tag.

NEIL1, a crucial participant in base excision repair, plays a pivotal role in addressing DNA damage induced by oxidation or exposure to mutagenic agents. Functioning as a DNA glycosylase, NEIL1 recognizes and eliminates damaged bases, exhibiting a preference for oxidized pyrimidines such as thymine glycol, formamidopyrimidine (Fapy), and 5-hydroxyuracil. Although it shows marginal activity towards 8-oxoguanine, NEIL1 excels in AP (apurinic/apyrimidinic) lyase activity, introducing nicks in the DNA strand. Through beta-delta elimination, it cleaves the DNA backbone, generating a single-strand break at the site of the removed base, encompassing both 3'- and 5'-phosphates. Notably, NEIL1 demonstrates DNA glycosylase/lyase activity towards mismatched uracil and thymine, particularly in U:C and T:C mismatches. Moreover, its specific binding to 5-hydroxymethylcytosine (5hmC) suggests that NEIL1 serves as a specialized reader of this modified DNA base.

Measured by its binding ability in a functional ELISA. Immobilized Human NEIL1 at 2 μg/mL (100 μL/well) can bind Anti- NEIL1 antibody, The ED₅₀ for this effect is 25.76 ng/mL.

Human

E. coli

C-His

Q96FI4 (M1-S390)

79661  [NCBI]

Full Length

MPEGPELHLASQFVNEACRALVFGGCVEKSSVSRNPEVPFESSAYRISASARGKELRLILSPLPGAQPQQEPLALVFRFGMSGSFQLVPREELPRHAHLRFYTAPPGPRLALCFVDIRRFGRWDLGGKWQPGRGPCVLQEYQQFRENVLRNLADKAFDRPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARSVLEALQQHRPSPELTLSQKIRTKLQNPDLLELCHSVPKEVVQLGGKGYGSESGEEDFAAFRAWLRCYGMPGMSSLQDRHGRTIWFQGDPGPLAPKGRKSRKKKSKATQLSPEDRVEDALPPSKAPSRTRRAKRDLPKRTATQRPEGTSLQQDPEAPTVPKKGRRKGRQAASGHCRPRKVKADIPSLEPEGTSAS

Approximately 45 kDa

≥ 80%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCl, 300 mM NaCl, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.