KLK11 Human

KLK11 is a 250 amino acid serine protease that consists of an 18 amino acid signal peptide and a 3 amino acid propeptide . The activation of KLK11 involves the removal of the propeptide region by thermolysin, resulting in the active form of the protease . The molecular weight of KLK11 is predicted to be 25.6 kDa, but due to glycosylation, it is observed to be approximately 41 kDa .

KLK11 is expressed in various tissues, including the prostate, trachea, salivary gland, lung, stomach, and skin . It plays a significant role in physiological processes, and growing evidence suggests its involvement in carcinogenesis . The enzyme’s specific activity is measured to be greater than 2200 pmoles/min/μg when using a colorimetric peptide substrate .

Recombinant KLK11 is produced in Human Embryonic Kidney 293 cells and purified through sequential chromatography . The purity of the recombinant protein is determined to be greater than 95% by SDS-PAGE analysis . The endotoxin level is maintained at less than 0.1 ng/μg .

The recombinant KLK11 is lyophilized and carrier-free . It is filtered before lyophilization through a 0.22-micron sterile filter to ensure sterility . For reconstitution, the lyophilized protein is recommended to be dissolved in sterile PBS to a concentration of 0.2–0.5 mg/mL . The reconstituted protein should be apportioned into working aliquots and stored at ≤ –20°C to avoid repeated freeze-thaw cycles .

The biological activity of KLK11 is assessed by its ability to cleave a colorimetric peptide substrate, D-Val-Leu-Lys-ThioBenzyl ester . The reaction is carried out in a specific buffer at 37°C, and the cleavage of the peptide substrate is measured at a wavelength of 405 nm .

Recombinant KLK11 is used in various cell culture applications and research studies to understand its role in physiological processes and its potential implications in diseases such as cancer .