In order to achieve high quality crystals, it is necessary to purify the raw material. In the present experimental study, the zone melting method was used to purify Lithium Flouride powder. A small amount of melt moves slowly from the solid area in order to remove impurities in the frozen solid. In this case, the number, size and length of the zone melting affect the final result, and cause the optimal distribution of solutes. At the beginning, the regional PURIFICATION system was equipped. The mechanism of work was moving furnace on a graphic crucible with full of LiF powder by 20 mm/h-1. This procedure was followed in a vacuum for 7, 9 and 14 times. At last the amounts of impurities such as Fe, Ba were measured by ICP (Inductively Coupled Plasma) analysis before and after PURIFICATION.

In order to gene cloning, at first desired gene should separate from other contaminants (proteins, primer-dimer bands unskilled, etc. ). Various physical and chemical methods were used for PURIFICATION of target gene from other contaminates; Here we have applied a new physical methods for PURIFICATION of gen from agarose gel under an electric field containing TAE. 1X fluid. We isolated PqHMGR form Panax quinquefoliusby using specific primers based on cDNA sequences. Ligation of isolated gene tovector and its cloning was done through E. coli (DH5α ). Finally, PqHMGR gene was purified by the foresaid device and after cloning in desired vector, extracted plasmid were sequenced for confirmation of gene PURIFICATION and cloning. Our resultd showed accuracy of this device in gene PURIFICATION.

Background: Placenta-specific 1 (PLAC1) is one of the recently-discovered Cancer-Testis-Placenta (CTP) antigen with restricted normal tissue and ectopic expression in a wide range of cancer cells from different histological origins. The production of recombinant human PLAC1 has already been optimized; however, no study has been reported so far on the production and PURIFICATION of mouse plac1. In this study, mouse plac1 expression and PURIFICATION was optimized in a prokaryotic system and the effects of the generated proteins on inducing humoral responses in mice were investigated. Methods: A fusion protein containing full extracellular domain of mouse plac1, immunostimulatory peptides, tetanus toxin P2P30 and PADRE and KDEL3 signal (main plac1), and the same fragment without immunostimulatory peptides (control plac1) was produced. To optimize production and PURIFICATION steps, different parameters including bacterial strain, cultivation temperature, cultivation time, IPTG concentration, culture medium, and also different buffers for PURIFICATION of the recombinant proteins were tested. After confirming the identity of recombinant plac1 proteins with Western Blotting (WB) and ELISA assays, these proteins were subcutaneously injected in mice with Freund's adjuvant and the anti-plac1 antibody response was detected by ELISA. Results: The optimal expression level of main and control plac1 was obtained in BL21 (DE3) and TB culture medium in the presence of 0. 25 mM IPTG after 24 hr of induction at 15 C. The buffer containing 2% sarkosyl produced higher yield and purity. Our results showed specific reactivity of anti-human recombinant plac1 polyclonal antibody with both main and control plac1 recombinant proteins in WB and ELISA analysis. Both proteins induced humoral responses in mice; however, anti-plac1 antibody titer was significantly higher in sera of mice immunized with main compared to control plac1. Conclusion: In this study, an optimized protocol for production and PURIFICATION of mouse plac1 was reported and it was shown that insertion of immunostimulatory peptides in gene construct could efficiently enhance humoral immune responses against mouse plac1, which could potentially augment cellular immune responses against plac1 leading to more effective anti-cancer responses.

On the one hand, the complexity of mental disorders and the undesirable use of different sciences, and the prevention and treatment of mental disorders, causes a move towards an interdisciplinary environment and the use of different sciences at the levels of health and treatment. Examples are physics and theories based on physics, biophysics and metaphysics, and quantum PURIFICATION. The method in this research is a developmental application that examines the effectiveness of quantum PURIFICATION at different levels of health with the aim of achieving purity and tranquility from the perspective of the Holy Quran, hadiths and related sciences. So the statements, propositions and metrics of quantum PURIFICATION need to be examined and evaluated in the field and validity. As a result of the effectiveness of the forty steps of purity and peace from the perspective of the Holy Quran, he has monitored the hadiths and sciences. These steps include skills such as smile, quantum rotation, power of thought, attraction, sleepclearing, wish-writing, concentration, worship, and eye-clearing, addiction, betrayal, hardship, poverty, jealousy, and objects, halflost attraction, calmness, control, and so on. Reducing unpleasant visual events, coding, patience, unity, control and management of the black box, time delay skills, reaching the white box, training and transfer of experiences, life spelling, creativity, color dreaming, verbal planning, communication with the source, goodness, spiritual light And optimism pointed out that cleansing and mental health pursue results.

Background: Interferon-gamma (IFN-γ ) is the most important cytokine in the immune system. This protein has been expressed in bacterial cells. However, bacterial cloning is not an easy task. We aimed to clone, express, and purify recombinant mouse IFN-γ and overcome problems in favor of commercial purposes. Materials and Methods: To amplify the gene product for cloning, we primarily designed two specific primers for the target gene. Following PCR amplification, the amplicon was inserted into the pET-21b(+) vector. The E. coli BL21 (DE3) CodonPlus strain was chosen for the expression of the target gene. Finally, the expressed recombinant mouse IFN-γ was assessed through the western blotting method. Results: We performed a cloning process and produced recombinant mouse IFN-γ in an optimal condition. We also noticed that monomeric protein could be transformed to a homodimeric structure which can be observed using the SDS PAGE (SDS-polyacrylamide gel electrophoresis) and western blotting. Conclusion: Experimental conditions strongly affect the large-scale cloning procedures required to be optimized in each laboratory. The expressed recombinant mouse IFN-γ described here is appropriate for commercial purposes.