Anti-Factor VIIa polyclonal Antibody

Purpose The purpose of this paper is to model the relationship between innovation systems players and markets to indicate the innovation functions behavior during the petrochemical technology life cycle. Design/methodology/approach In a general classification, innovation systems are divided into four categories: technical, sectoral, regional and national. If two approaches are hybrid, their benefits would be combined. According to the sectoral structure of the governance model in Iran, in many sectors, such as petrochemical technology, the combination of one another with a sectoral approach is essential. Hence, this paper has introduced a new hybrid approach, called a techno-sectoral innovation system, and has used system dynamics as a methodology and a petrochemical industry as a case study. Findings The results predict the functions state of the innovation system and detect activation of innovation motors in each stage of innovation life cycle. Validation is investigated using Monte Carlo simulation that shows the error of the indices is acceptable. It can be concluded that the model is relatively in a development state and the motor of entrepreneurship functions. Originality/value This case-based model can help other researchers, as a generic model. It could be customized with the input parameters and relational flows of new cases, and functions (F1-F7) can show the result of each scenario made by the innovation analyst and the policymaker.

Factor VII (FVII) is a key serine protease in blood coagulation. N-glycosylation in FVII has been shown to be critical for protein secretion. To date, however, the underlying biochemical mechanism remains unclear. Recently, we found that N-glycans in the transmembrane serine protease corin are critical for calnexin-assisted protein folding and extracellular expression. In this study, we tested the hypothesis that N-glycans in the FVII protease domain mediate calnexin-assisted protein folding and that naturally occurring F7 mutations abolishing N-glycosylation impair FVII secretion. We expressed human FVII wild-type (WT) and mutant proteins lacking one or both N-glycosylation sites in HEK293 and HepG2 cells in the presence or absence of a glucosidase inhibitor. FVII expression, secretion and binding to endoplasmic reticulum chaperones were examined by immune staining, co-immunoprecipitation, Western blotting, and ELISA. We found that N-glycosylation at N360 in the protease domain, but not N183 in the pro-peptide domain, of human FVII is required for protein secretion. Elimination of N-glycosylation at N360 impaired calnexin-assisted FVII folding and secretion. Similar results were observed in WT FVII when N-glycan-calnexin interaction was blocked by glucosidase inhibition. Naturally occurring F7 mutations abolishing N-glycosylation at N360 reduced FVII secretion in HEK293 and HepG2 cells. These results indicate that N-glycans in the FVII protease domain mediate calnexin-assisted protein folding and subsequent extracellular expression. Naturally occurring F7 mutations abolishing N-glycosylation in FVII may impair this mechanism, thereby reducing FVII levels in patients.