nei 1

SerpinB1 is an endogenous inhibitor of serine proteases recognized for its anti-inflammatory and host-protective properties. Serum SerpinB1 levels are elevated in patients with type 2 diabetes compared with that in healthy subjects and are negatively correlated with serum LDL-C. serpinB1 as an endogenous protein that can potentially be harnessed to enhance functional beta cell mass in patients with diabetes.

NEIL1 is a member of DNA glycosylases. DNA glycosylases are a family homologous to the bacterial Fpg/Nei family. They play a role in base excision repair which is the mechanism by which damaged bases in DNA are removed and replaced. The first step of this process is catalyzed by DNA glycosylases. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an AP site. NEIL1 functions in base excision repair of DNA damaged by oxidation or by mutagenic agents. It acts as a DNA glycosylase that recognizes and removes damaged bases. NEIL1 prefers to oxidized pyrimidines, such as thymine glycol, Formamidopyrimidine (Fapy), and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. It has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand and 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.