Human Pancreasin/Marapsin/PRSS27 (His Tag) recombinant protein

Human Pancreasin/Marapsin/PRSS27 (His Tag) recombinant protein

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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.

Serine protease 27

PRSS27; MARAPSIN; NQ1884/PRO4327; CAPH2; MPN; PANCREASIN

Q9BQR3

PRSS27; MPN; UNQ1884/PRO4327

Human Cells

A DNA sequence encoding the human PRSS27 (Q9BQR3) extracellular domain (Met 1-Lys 290) was expressed, fused with a polyhistidine tag at the C-terminus.

Human

The recombinant human PRSS27 consists of 279 amino acids and has a predicted molecular mass of 30.9 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh PRSS27 is approximately 42 kDa due to glycosylation.

> 95 % as determined by SDS-PAGE

Measured by its ability to cleave a colorimetric peptide substrate, NcarbobenzyloxyGlyArgThioBenzyl ester (ZGR-SBzl), in the presence of 5,5’Dithiobis (2-nitrobenzoic acid) (DTNB).
The specific activity is > 2000 pmols/min/μg.