Human glandular kallikrein 2 (KLK2)

Human glandular kallikrein 2 (KLK2) is a tryptic serine protease predominantly expressed in prostatic tissue and secreted into prostatic fluid, where it plays a role in cleaving seminal clotting proteins and facilitating sperm liquefaction[1][2][5][6]. KLK2 is closely related to prostate-specific antigen (KLK3) and belongs to the classical kallikrein family, mapping to the chromosomal locus 19q13.4 and sharing structural features with other tissue kallikreins[2][3]. It is regulated by steroid hormones, subject to reversible inhibition by zinc, and associated with prostate cancer both as a biomarker and a molecule of research interest[1][2][3]. KLK2's activity is regulated in part by its extended regulatory loop structures, such as the 99-loop, which also serves as a modulator of inhibitor binding and inactivation[1].

Other names

Human kallikrein 2Kallikrein-2KLK2Glandular kallikrein 2

Protease inhibition (irreversible or reversible small-molecule inhibition of the enzymatic activity through binding to the active site or regulatory loops, such as the 99-loop) Inhibitors (such as Zn²⁺ or small molecules) prevent KLK2 from cleaving protein substrates