Recombinant Mouse MCPT6/Mast Cell Protease-6 Protein (His Tag) | PKSM041266

Recombinant Mouse MCPT6/Mast Cell Protease-6 Protein (His Tag) | PKSM041266 | Gentaur US, UK & Europe Disrtribition

Synonyms: Tryptase beta-2; Tryptase-2; Mast cell protease 6; mMCP-6; Tpsb2

Active Protein: N/A

Activity: Recombinant Mouse MCPT6 is produced by our Mammalian expression system and the target gene encoding Ala23-Ser276 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Mouse MCPT6 is produced by our Mammalian expression system and the target gene encoding Ala23-Ser276 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-His

Species: Mouse

Expressed Host: Human Cells

Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg as determined by the LAL method.

Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.

Molecular Mass: 29.3 kDa

Formulation: Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mMNacl, pH 7.5.

Reconstitution: Not Applicable

Background: 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.

Research Area: N/A