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.