Mouse/Rat Kallikrein 7 Antibody

KLK7 (Kallikrein 7; also Serine protease 6, Thymopsin and Stratum corneum chymotryptic enzyme/SCCE) is a 27 kDa (predicted), secreted glycoprotein member of the kallikrein subfamily, peptidase S1 family of enzymes. It is an IL-4 and IL-13-inducible chymotrypsin-like serine protease that has restricted expression, being associated with stratum spinosum and granulosum keratinocytes, distal and proximal convoluted tubule epithelium, limited pancreatic acinar cells. In contrast, KLK7 is widely expressed by a variety of carcinoma cell types. KLK7 preferentially cleaves peptide bonds that contain an aromatic (Tyr or Phe) residue in the P1 (or postcleavage C-terminal amino acid) position. Molecules known to serve as substrates for KLK7 include chemerin, fibronectin, E-cadherin, LL37, procaspase-14, MMP-9 and desmoglein. The nature of the KLK7 substrates indicates that it plays a key role in intercellular adhesion dissolution with subsequent cell migration. Mouse KLK7 is synthesized as a 249 amino acid (aa) precursor. It contains a 21 aa signal sequence, a four aa prosegment, and a 224 aa mature region (aa 26-249). The mature molecule contains one large protease domain (aa 26-246) and a variable, three aa C-terminus that possesses either a VSW or ASR motif. Over aa 22-249, mouse KLK7 shares 75% and 85% aa sequence identity with human and hamster KLK7, respectively.