prss 6

Human Kallikrein 7 is a member of the tissue kallikrein family of extracellular serine proteases that is made up of 15 members. It is predominantly expressed in the skin. A major physiological function of Kallikrein 7 is to regulate the desquamation process (the shedding of corneocytes from the outer layer of the epidermis) through proteolysis of the intercellular adhesive structures between corneocytes. Dysregulation of Kallikrein 7 has been linked to several inflammatory skin diseases including atopic dermatitis, psoriasis, and Netherton syndrome. Studies have shown that Kallikrein 5 is a potential physiological activator for Kallikrein 7. The proform of Kallikrein 7 can be activated by thermolysin.

KLK6 (kallikrein-related peptidase 6), also known as Klk7, belongs to the peptidase S1 family, Kallikrein subfamily. Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. KLK6 is a serine protease that exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Klk7 shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein, and extracellular matrix proteins such as fibronectin, laminin, vitronectin, and collagen. KLK6 degrades alpha-synuclein and prevents its polymerization, indicating that KLK6 may be involved in the pathogenesis of Parkinson's disease and other synucleinopathies. Klk7 may be involved in the regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis.

Kallikrein 7/KLK7 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 26.7 kDa and the accession number is A0A024R4H6.