KLK5 Human

The human KLK5 gene encodes a protein that consists of a signal peptide (Met1 to Gly22), a pro region (Val23 to Arg66), and a mature/active enzyme (Ile67 to Ser293) . The mature form of KLK5 is responsible for its proteolytic activity. KLK5 is initially synthesized as an inactive zymogen and requires proteolytic cleavage to become active .

KLK5 is predominantly expressed in the skin, particularly in the stratum corneum, where it plays a crucial role in the degradation of corneodesmosomes, leading to skin desquamation . This process is essential for maintaining skin homeostasis and barrier function. Additionally, KLK5 has been implicated in various pathological conditions, including atopic dermatitis, rosacea, and certain types of cancer .

Recombinant human KLK5 is produced using advanced biotechnological methods. It is typically expressed in a mouse myeloma cell line (NS0) and purified to high levels of purity (>95%) using SDS-PAGE under reducing conditions . The recombinant protein is often tagged with a C-terminal 10-His tag to facilitate purification and detection .

The activity of recombinant KLK5 is measured by its ability to cleave specific fluorogenic peptide substrates, such as Boc-VPR-AMC . This activity is quantified in terms of specific activity, which is typically greater than 200 pmol/min/µg .

Recombinant KLK5 is widely used in research to study its role in skin physiology and pathology. It is also utilized in the development of therapeutic interventions for skin disorders and certain cancers. The availability of high-purity recombinant KLK5 allows researchers to investigate its biochemical properties, substrate specificity, and potential inhibitors .