Marapsin Proteins, Antibodies, cDNA Clones, ELISA Kits Research Reagents

PRSS27 (Serine Protease 27) is a protein coding gene located on human chromosome 16p13.3. PRSS27 is also known as MPN and CAPH2. The human PRSS27 gene encodes a 31940 Da protein containing 290 amino acids. The PRSS27 protein is biasedly expressed in esophagus and skin. PRSS27 is related to serine-type endopeptidase activity. PRSS33 is an important paralog of PRSS27 gene. PRSS27 is associated with some diseases, such as Necrotizing Gastritis.

Marapsin Protein (1)

    Marapsin Antibody (6)

      Marapsin ELISA Kit & Match Antibody ELISA Pair Set (1)

      Marapsin cDNA Clone (13)


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      Marapsin Lysate (1)

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        Marapsin Background

        The name "Pancreasin" because it is transcribed strongly in the pancreas. This secreted, tryptic serine protease, also known as Marapsin or PRSS27 (Protease, serine, 27), is a member of the peptidase S1 family. Pancreasin is inhibited by benzamidine and leupeptin but resists several classic inhibitors of trypsin. Marapsin was constitutively expressed in nonkeratinizing stratified squamous epithelia of human esophagus, tonsil, cervix, larynx, and cornea. In fact, marapsin was the second most strongly up-regulated protease in psoriatic lesions, where expression was localized to the upper region of the hyperplastic epidermis. Similarly, in the hyperproliferative epithelium of regenerating murine skin wounds, marapsin localized to the suprabasal layers, where keratinocytes undergo squamous differentiation. Marapsin's restricted expression, localization, and cytokine-inducible expression suggest a role in the terminal differentiation of keratinocytes in hyperproliferating squamous epithelia.

        Marapsin References

        • Bhagwandin VJ, et al. (2003) Structure and activity of human pancreasin, a novel tryptic serine peptidase expressed primarily by the pancreas. J Biol Chem. 278(5): 3363-71.
        • Li W, et al. (2009) The serine protease marapsin is expressed in stratified squamous epithelia and is up-regulated in the hyperproliferative epidermis of psoriasis and regenerating wounds. J Biol Chem. 284(1): 218-28.

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