Latexin Human

Recombinant human latexin is typically expressed in E. coli with an N-terminal His tag. The protein consists of amino acids Glu2-Glu222 . The molecular weight of latexin is predicted to be around 27 kDa, but it migrates to 30-35 kDa based on Bis-Tris PAGE results .

Latexin is expressed in small nociceptive neurons in sensory ganglia and in a subset of neurons in the telencephalon . It was initially identified as a marker of neurons in the lateral neocortex of the developing brain .

Latexin inhibits carboxypeptidase A1 by preventing the cleavage of the colorimetric peptide substrate Ac-Phe-Thiaphe-OH in the presence of 5,5’-Dithio-bis (2-nitrobenzoic acid) (DTNB). The IC50 value for this inhibition is less than 1 nM .

Recent studies have identified the latexin (LXN) gene as a potential tumor suppressor in several types of solid tumors and lymphoma. The expression of LXN is often absent or downregulated in leukemic cells . This suggests that latexin could play a significant role in cancer biology and might be a target for therapeutic interventions.

Recombinant human latexin is typically lyophilized from a 0.22 µm filtered solution in PBS (pH 7.4) with 8% trehalose added as a protectant before lyophilization . The reconstituted protein is stable at -80°C for up to 12 months and at 4°C for up to one week. It is important to use a manual defrost freezer and avoid repeated freeze-thaw cycles to maintain the protein’s stability .

Due to its inhibitory properties, latexin is used in various biochemical assays to study carboxypeptidase activity. It is also being explored for its potential therapeutic applications in cancer treatment due to its tumor suppressor functions .