KLK2 Human

KLK2 is a secreted enzyme that is highly specific for cleavage after arginine residues . The enzyme is synthesized as an inactive precursor and undergoes proteolytic cleavage to become active. The active form of KLK2 can activate the urokinase-type plasminogen activator, which is involved in the breakdown of blood clots . Additionally, KLK2 is structurally related to KLK3, also known as prostate-specific antigen (PSA), and both are considered biomarkers for prostate cancer .

Recombinant human KLK2 is produced using various expression systems, including bacterial, yeast, and mammalian cells. One common method involves the use of mouse myeloma cell lines (NS0) to produce KLK2 with a C-terminal His-tag for easy purification . The recombinant protein is typically purified using chromatographic techniques to achieve high purity levels, often greater than 85% .

KLK2 is used in various research and clinical applications. It is employed as a biomarker for prostate cancer diagnosis and monitoring. Additionally, KLK2 is used in enzymatic assays to study its activity and interactions with other proteins. The enzyme’s ability to cleave specific peptide substrates makes it valuable in biochemical research .

Recombinant KLK2 is supplied as a filtered solution in sodium citrate and NaCl. It is shipped with dry ice to maintain stability and should be stored at -70°C to prevent degradation. The protein remains stable for up to six months when stored under these conditions .