Background: Serine proteases are important in many biological processes such as receptor activation, complement activation, coagulation and tissue remodeling. Pancreasin, also known as marapsin (MPN), channel activating protease 2-like protein (CAPH2) or protease, serine 27, is an N-glycosylated, secreted pancreatic tryptic serine peptidase and proteinase. Pancreasin is responsible for cleaving peptides after an arginine residue and may play a role in regulating cell growth and migration. It can be inhibited by benzamidine and Leupeptin. Pancreasin is closely related to prostatin, tryptase-g, Testisin and tryptase-e. These proteins share approximately 40% amino acid identity with tryptase-a and tryptase-b. They contain Cysteine residues that may form a disulfide link bewteen the propeptide and catalytic chain, a tryptic propeptide cleavage site and a C-terminal membrane anchor. Tryptase-e and the human Pancreasin protein lack the characteristic C-terminal membrane anchor.
Description: Rabbit polyclonal to Marapsin1
Immunogen: KLH conjugated synthetic peptide derived from Marapsin1
Specificity: ·Reacts with Human, Mouse and Rat.
.·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 32 kDa;
·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;
·Immunocytochemistry/Immunofluorescence: 1/100;
·Immunoprecipitation: 1/50;
·ELISA: 1/500;
·Optimal working dilutions must be determined by the end user.
