Application:IF
Reactivity: Rat (predicted: Human,Mouse,Pig,Cow,Dog)
The human tissue Kallikrein gene family encodes 15 serine proteases. All Kallikreins share structural similarities including cysteine residues, a catalytic triad of His, Asp, and Ser residues, typically five coding exons and varied intron phases. Kallikreins are predominantly secreted as inactive zymogens prior to activation by cleavage of an N-terminal peptide and all function extracellularly. Kallikreins can be activated autocatalytically, via other Kallikreins, or additional proteases. While structurally similar, Kallikrein family members have distinct functions and have key roles in many physiological and pathological processes. Many human tissue Kallikreins also show promise as cancer biomarkers, which may facilitate earlier detection and characterization of many forms of cancer.
Kallikrein 7, also known as stratum corneum chymotryptic enzyme (SCCE) and PRSS6, is a chymotrypsin-like serine proteinase. Originally described from human skin as a serine protease involved in shedding of skin cells and remodeling if the skin, SCCE was later identified as Kallikrein 7. Kallikrein 7 is found at the highest levels in the skin, often complexed with the endogenous serpins SLPI or elafin and kallikrein 7 can be found complexed to a number of different proteinase inhibitors. In addition to skin, Kallikrein 7 has been found in the kidney, esophagus, neuronal tissues, amniotic fluid, saliva, breast milk, urine, synovial fluid, seminal plasma and serum. Kallikrein 7 has been reported to be decreased in the CSF of Alzheimer's patients and message levels of KLK7 were decreased in adenocarcinoma. In skin, overexpression of hK7 has been shown to cause a form of dermatitis and in psoriasis hK7 is expressed in higher levels than controls. The skin adhesive proteins corneodesmosin and desmocollin 1 have been reported to be substrates of Kallikrein 7, as is interleukin 1 and the insulin B-chain.