Analysis Biomolecular Interactions of Antibody with Kallikrein-related Peptidase 7 (KLK7) by BLI (CAT#: STEM-MB-0100-CJ)

Introduction

Kallikrein-related peptidase 7 (KLK7) is a serine protease that in humans is encoded by the KLK7 gene. KLK7 was initially purified from the epidermis and characterised as stratum corneum chymotryptic enzyme (SCCE). KLK7 is secreted as an inactive zymogen in the stratum granulosum layer of the epidermis, requiring proteolytic cleavage of the short N-terminal pro-region to liberate activated enzyme. Once active, KLK7 is able to cleave desmocollin and corneodesmosin. These proteins constitute the extracellular component of corneodesmosomes, intercellular cohesive structures which link the intermediate filaments of adjacent cells in the stratum corneum. Proteolysis of corneodesmosomes is required for desquamation, the shedding of corneocytes from the outer layer of the epidermis. KLK7 expression is highly downregulated at acral surfaces where desquamation is delayed and the epidermis is thick. Both KLK5 and KLK14, other skin-expressed proteases, also cleave corneodesmosomal proteins.