In other words, the concentration of endogenous salusin-a is lower than salusin-b in the case of atherosclerosis. In light of the same doses of salusin-a and salusin-b used in the current study. Secondly, we did not get the results of MCP-1 protein expression assayed by western blotting since the anti-MCP-1 antibody did not work well. In addition, by salusin-b and the alleviation of atherosclerosis by salusin-a. In summary, the present study found that exogenous salusin-b, but not salusin-a, could directly promote vascular inflammation in apoE-/- mice via the I-kBa/NF-kB pathway, resulting in the aggravation of atherosclerosis. Wu et al. reported that MPF activity in goat oocytes is significantly increased following DEM treatment. In mice, the majority of active MPF is localized at the metaphase plate and is therefore not present in enucleated oocytes, which are used as recipient cytoplasts during nuclear transfer. Most studies in mammals suggest that drug treatments can maintain high MPF activity in mature oocytes. Oocytes enucleated using DEM have developed into live piglets; however, the effect of DEM treatment on MPF activity in enucleated porcine oocytes has not been examined. The present study investigated the effect of DEM treatment on the level of MPF and the distribution of cyclin B1 in mature porcine oocytes. DEM-assisted enucleation was compared with mechanical enucleation in terms of the ability of embryos to develop normally following SCNT. MBP-tagged proteins can be easily purified with commercially available MBP-binding columns. PDI forms and breaks disulfide bonds of proteins in the lumen of the endoplasmic reticulum. The cytoplasm is usually a reducing environment that prevents proper disulfide bond formation, but PDI increases the production of soluble proteins in both the cytoplasm and periplasm of E. coli. PDI is composed of four thioredoxin-like domains, named a, b, b’, and a’. The a and a’ domains display redox-active catalytic and chaperone activities, whereas the b and b’ domains only demonstrate some chaperone functions. Previous experiments in our laboratory have shown that PDIb’a’ increases the solubility of several proteins to the same degree as PDI ; however, the data presented here show that PDIb’a’ GANT61 500579-04-4 was less effective than PDI at solubilizing hGCSF. NusA was suggested as a solubilizing tag protein based on the revised Wilkinson-Harrison solubility model, which predicted NusA to be 95% soluble and to improve the solubility of several proteins. PDI and PDIb’a’ were also predicted to be good solubilizing agents according to this model. The revised Wilkinson-Harrison solubility model considers the number of four turn-forming residues and determines the net charge by subtracting the number of acidic residues from the number of basic residues. However, this model may have some limitations because it predicted relatively low solubility for the MBP, Trx, and GST tags, despite the fact that hGCSF fused with these tags showed good solubility.