trypsin-like

Transmembrane Protease Serine 11B (TMPRSS11B) is a single-pass type II membrane protein member of the peptidase S1 family. TMPRSS11B contains one peptidase S1 domain and one SEA domain. TMPRSS11B is a serine protease that may play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions.

Probable serine protease which may play a role in cellular senescence. Overexpression inhibits cell growth and induce G1 cell cycle arrest.

Chymotrypsin-Like Elastase Family Member 3A (CELA3A) is an enzyme that contains one peptidase S1 domain. ELA3A belongs to the peptidase S1 family of the Elastase subfamily. ELA3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. ELA3A may also function in the intestinal transport and metabolism of cholesterol. ELA3A is efficient protease with alanine specificity but only little elastolytic activity. ELA3A preferentially cleaves proteins after alanine residues.

Serine protease of trypsin-like cleavage specificity. Synthesized in a zymogen form, proacrosin and stored in the acrosome. Acrosin Protein, Meleagris gallopavo, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 43.1 kDa and the accession number is Q2UVH8.

Contrapsin inhibits trypsin-like proteases. Serpin A3K Protein, Mouse, Recombinant (His) is expressed in yeast with C-6xHis tag. The predicted molecular weight is 45.7 kDa and the accession number is P07759.

Tissue kallikrein 13 (hK13), also known as KLK-L4 (kallikrein-like gene 4), is a member of the human tissue kallikrein family of serine proteases having diverse physiological functions in many tissues. The KLK13 gene resides on chromosome 19q13.3-4 along with other 14 members in a gene cluster and shares a high degree of homology. KLK13 is a trypsin-like, secreted serine protease expressed specifically in the testicular tissue including prostate, salivary gland, breast, and testis. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and may play a role in metastasis. KLK13 may be involved in the pathogenesis and/or progression of breast and ovary cancers and is regarded as a novel cancer biomarker. Besides, KLK13 interacts and forms complexes with several serum protease inhibitors, such as alpha2-macroglobulin, and its expression is regulated by steroid hormones.

Tryptases are serine proteases with trypsin-like specificity. Together with chymases and Cathepsin G, tryptases are important players in mast cell mediation of inflammatory and allergic responses. Tryptase alpha/beta-1(TPSAB1), also known as mast cell protease 7 (MCPT7), it exhibits anticoagulant activity due to its ability to degrade fibrinogen in the presence of a diverse array of protease inhibitors in plasma. The two Isoform 1 and isoform 2 are expressed in lung, stomach, spleen, heart and skin; in these tissues, isoform 1 is predominant. Isoform 2 is expressed in aorta, spleen, and breast tumor, with highest levels in the endothelial cells of some blood vessels surrounding the aorta, as well as those surrounding the tumor and low levels, if any, in mast cells. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates. It may play a role in innate immunity.

Tryptases are Trypsin-like Serine Proteases. β-Tryptases are the main isoenzymes in mast cells. Βtryptases form active tetramers with heparin proteoglycan. In the tetramer, the unique arrangement of the active sites facing a narrow central pore, β-Tryptases are resistant to macromolecule protease inhibitors . When mast cells are activated, β-Tryptases are released and participate in provoking inflammatory conditions . β-Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic disorders.