protein

NEIL1 Protein, Human (His)

HY-P74734

5 μg;10 μg;50 μg

60;100;280 USD

NEIL1 Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg

60;100;280 USD

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. The total length of NEIL1 Protein, Human (His) is 390 a.a., with molecular weight of ~45 kDa.

Human

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.

Endonuclease 8-like 1; Endonuclease VIII-like 1; FPG1; NEH1; NEIL1

Greater than 84% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 8.0.

Room temperature in continental US; may vary elsewhere.