Marapsin Protein, Human, Recombinant (His Tag): Product Information
> 95 % as determined by SDS-PAGE
< 1.0 EU per μg of the protein as determined by the LAL method
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.
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.
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.
Lyophilized from sterile PBS, pH 7.4 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
CAPH2 Protein, Human; MPN Protein, Human; UNQ1884/PRO4327 Protein, Human
Marapsin Background Information
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.
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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