Latexin was initially identified as a molecular marker for the regional specification of the neocortex in the developing brain of rats . It is highly expressed in various tissues, including the heart, prostate, ovary, kidney, pancreas, and colon . The protein plays a crucial role in inhibiting carboxypeptidase A1, an enzyme involved in protein degradation .
The recombinant mouse latexin protein is typically expressed in E. coli and consists of 228 amino acids with a calculated molecular mass of approximately 26.3 kDa . When analyzed under reducing conditions using SDS-PAGE, the apparent molecular mass is around 32 kDa . The protein is often tagged with a polyhistidine tag at the N-terminus to facilitate purification .
Latexin’s activity is measured by its ability to inhibit carboxypeptidase A1 cleavage of the colorimetric peptide substrate Ac-Phe-Thiaphe-OH in the presence of 5,5’-dithiobis (2-nitrobenzoic acid) (DTNB) . The IC50 value, which indicates the concentration required to inhibit 50% of the enzyme activity, is less than 2.0 nM .
Recombinant mouse latexin is used in various biochemical and physiological studies to understand its role in enzyme inhibition and its potential therapeutic applications . The protein is typically lyophilized and stored under sterile conditions at -20°C to -80°C to maintain stability . It is recommended to avoid repeated freeze-thaw cycles to preserve its activity .