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

All Marapsin reagents are produced in house and quality controlled, including 6 Marapsin Antibody, 1 Marapsin ELISA, 13 Marapsin Gene, 1 Marapsin IP Kit, 1 Marapsin Lysate, 1 Marapsin Protein, 1 Marapsin qPCR. All Marapsin reagents are ready to use.

Marapsin Protein (1)

    Marapsin Antibody (6)

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

      Marapsin cDNA Clone (13)

      NM_031948.3

      Marapsin qPCR Primer (1)

      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), which 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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