TPSAB1, namely tryptase alpha/beta-1, is a serine protease with trypsin­like activity. TPSAB1 is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. It may play a role in innate immunity. Diseases associated with TPSAB1 include mastocytosis and systemic mastocytosis.

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.

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.

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. TPSB2 Protein, Human, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 31.4 kDa and the accession number is P20231.

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. TPSAB1 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 30.1 kDa and the accession number is Q02844.

Tryptase beta-2(Tpsb2), also known as Mast cell protease 6(mMCP-6), belongs to the peptidase S1 family and Tryptase subfamily. Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. It plays a role in innate immunity. Tpsb2 can be detected primarily in skin during embryogenesis. Tpsb2 can not be detected at early embryonic stages but is abundantly expressed in later stages with a peak at E17.5-E18.5. Tryptase is a homotetramer. The active tetramer is converted to inactive monomers at neutral and acidic pH in the absence of heparin. Low concentrations of inactive monomers become active monomers at pH 6.0 in the presence of heparin. When the concentration of active monomers is higher, they convert to active monomers and then to active tetramers. These monomers are active and functionally distinct from the tetrameric enzyme. In contrast to the hidden active sites in the tetrameric form, the active site of the monomeric form is accessible for macromolecular proteins and inhibitors eg: fibrinogen which is a substrate for the monomeric but not for the tetrameric form. The monomeric form forms a complex with SERPINB6.

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. TPSB2 Protein, Human, Recombinant (His & Myc) is expressed in yeast with C-6xHis-Myc tag. The predicted molecular weight is 31.2 kDa and the accession number is P20231.

N/A. BSSP-4 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 35.9 kDa and the accession number is Q9ER10.

Brain-Specific Serine Protease 4 (BSSP-4) is a serine protease that preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. BSSP-4 is expressed abundantly in the epithelial cells of the airways, including trachea, esophagus and fetal lung, but scarce in adult lung and expressed at low levels in placenta, pancreas, prostate and thyroid gland. BSSP-4 belongs to the peptidase S1 family and related to trypsin, referentially hydrolyzing substrates after arginine and lysine residues. However, BSSP-4 is less susceptible to inhibition by common trypsin inhibitors such as aprotinin, α1-antitrypsin and secretory leukocyte protease inhibitor. BSSP-4 efficiently converts pro-urokinase- type plasminogen activator to its mature, active form.

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. TPSAB1 Protein, Rat, Recombinant (His & Myc & SUMO) is expressed in E. coli expression system with N-10xHis-SUMO and C-Myc tag. The predicted molecular weight is 47.4 kDa and the accession number is P27435.

Protein AMBP belongs to the calycin superfamily and Lipocalin family. AMBP can be cleaved into three chains: α-1-microglobulin, inter-α-trypsin inhibitor light chain and trypstatin. AMBP is expressed by the liver and secreted in plasma. α-1-microglobulin occurs in many physiological fluids including the plasma, urine, and cerebrospinal fluid. Inter-α-trypsin inhibitor is present in the plasma and urine. α-1-microglobulin occurs as a monomer and also in complexes with IgA and albumin, Inter-α-trypsin inhibitor inhibits trypsin, plasmin and lysosomal granulocytic elastase. Trypstatin act as a trypsin inhibitor, exists in a monomer forms and also occurs as a complex with tryptase in mast cells.