Introduction: Mandibular deficiency is one of the most common malocclusions that is treated with functional appliances during growth periods. The aim of this study was to evaluate the histologic changes of the single local injection of rBMP2 in combination with bite jumper therapy in a rabbit model TMJ.Materials & Methods: Eighteen 8-week old Albino New Zealand white male rabbits were divided into three groups: The first group served as control and in the second and third groups rBMP2 and normal saline were injected respectively. The second and third groups had bite jumper appliance. After 8-weeks of bite jumper therapy, in the second group 12.5mgr rBMP2 powder plus 2.5cc normal saline and in the third group only 2.5 cc normal saline was injected in the TMJs on both sides. After 16-weeks of treatment, the animals were sacrificed and the joints were examined histologically.Results: The rBMP2 group showed greater cartilage cells and maximum condylar cartilage thickness (in the form of cartilage hyperplasia) than control and normal saline groups. The control group had the lowest disc deformity histologically and the rBMP2 group showed lower disc deformity than normal saline group.Conclusion: rBMP2 is able to accelerate condylar cartilage growth in the form of cartilage hyperplasia.

Background: Streptokinase (SK) is most widely used for treatment of myocardial infarction, however, it is the most expensive thrombolytic agent. A major drawback to SK use is the widespread presence of anti–streptokinase antibodies (Abs). These Abs cause allergic reactions and neutralize streptokinase therapeutic effects.Materials and methods: To produce an engineered variant of streptokinase being functional and less antigenic than the native molecule, we cloned and expressed streptokinase mutant gene lacking the C-terminal 42 amino acids. RECOMBINANT PROTEIN was confirmed by western blot analysis with anti T7 monoclonal antibodies.Results: pGEMEX-1 expression vector contains T7 gene 10 PROTEIN as fusion PROTEIN immediately downstream of T7 promoter and before multiple cloning site, streptokinase mutant gene was cloned after fusion PROTEIN.Conclusion: We cloned and expressed mutant streptokinase gene, lacking the C-terminal 42 amino acids. If mut-C42 activity was less affected by neutralizing antibodies compared with native streptokinase, this engineered variant could be a preferred alternative to native streptokinase for thrombolytic therapy.

The low level expression of transgenes and their silence through successive generations are the most important factors limiting the production of RECOMBINANT PROTEINs in plants. Choosing an appropriate plant tissue for expression, and improving of the gene cassette could increase the expression of the transgene transferred to the plant. To address this problem, in this study, the increase of expression level of GUS gene in tobacco seed was considered by designing and preparation of seed specific construct and transferring it into the tobacco explents. The signal sequence in upstream and KDEL in downstream of the GUS gene were integrated as signals for PROTEIN retention in endoplasmic reticulum. The matrix attachment region (MAR) sequence was placed downstream of the GUS gene to prevent silencing. The whole fragment was expressed under the control of Napin, the seed specific promoter. This construct was transferred to A.tumefaciens LBA4404 and then used to transform tobacco leaf explants. Analysis of regenerated plants by using PCR and specific primers of nptII and GUS indicated the successful transfer of these genes to plantlets. The RT-PCR reaction results showed that nptII is transcribed in both tissues while GUS is only transcribed in the seed tissue. This finding is expected when considering that Nos promoter (which controls the nptII transcription) is a constitutive and Napin is a seed specific promoter. Expression of GUS in seeds of selected plants was investigated using SDS-PAGE and histochemical assay. The nearly 60 kDa band in the transgenic plant sample and also the results of histochemical assay indicate the expression of GUS gene in transgenic seeds of tobacco.

Introduction: Production of antibodies against specific PROTEINs of testis germ cells is of great significance for the investigation of processes involved in spermatogenesis, study of infertility problems and determination of the probable role of these PROTEINs as cancer-testis antigens. Murine Testis Specific RECOMBINANT PROTEIN 101 (mTEX101) is a 38kDa, GPI-anchored PROTEIN which is expressed in testis germ cells of adult mice but it seems to be absent in other tissues. The structure and function of mTEX101 is not completely understood yet, but it is speculated that it may transducer biochemical signals into the cytoplasm since mTEX101 does not have an intracellular domain but the precise mechanisms are still ambiguous.Materials and Methods: RNA was extracted from three adult mice testis. The RNA was used in RT-PCR, employing a pair of specific primers for mTEX101 ORF region. TA-cloning technique was performed by the insertion of mTEX101 into a pGEM-T Easy Vector, followed by its sub cloning into a His-tagged expression vector, pET-28a (+). The RECOMBINANT mTEX101 was then produced by transfection of the expression vector into BL 21 (DE3) E. coli strain. Results: A RECOMBINANT PROTEIN, weighing 27kDa, was produced upon IPT Ginduction of the bacterial host. The presence of mTEX101 PROTEIN was detected through Western blot analysis by anti-mTEX101 peptide antibodies. Conclusion: We produced mTEX101 RECOMBINANT PROTEIN that could be used for the production of mono and polyclonal antibodies.

Background: Helicobacter pylori (H. pylori) is a gram negative bacilli that causes the stomach and duodenum diseases in human. An important virulence factor of H. pylori is CagA gene which increases the colonization in stomach epithelial cells and lead to inflammation and peptic ulcers. The aim of the present study was to produce RECOMBINANT PROTEIN containing highly antigenic region of CagA in E. coli.Materials and Methods: In this experimental study, the antigenic region of CagA gene with 1245 base pair was detected by bioinformatics methods, proliferated by PCR method, digested by BamHI and XhoI restriction enzymes and cloned into pET32a plasmid and was expressed in theE. coli BL21 (DE3) pLysSwith induction by IPTG. The expressed PROTEIN was purified with Ni-NTA kit and its antigenicity was studied by western blotting method.Results: Data showed the successful cloning and expression of the target gene. In western blotting, the produced PROTEIN interacted with infected human and mice sera.Conclusion: Results indicated that RECOMBINANT CagA PROTEIN (65 KDa) maintained its antigenicity, so could be used for serological diagnosis of H. pylori diseases and production of vaccine.

Objective: With considering about our extended information in genome sequence field which gathered in genome data banks nowadays discovering the genes function and their products still unclear that’s why study in this area sensed. Proteomics researches are one of the powerful tools for reach to this knowledge.Materials and Methods: In our study at first we prepare competent cells from Escherichia coli species named BL21 for expressing RECOMBINANT PROTEIN, then in several stages, essential condition for processing RECOMBINANT PROTEIN, of this sort; change in culture temperature, induction time and concentration of IPTG for PROTEIN expression, time and number of sonication pulses for breaks in bacterial membrane and releasing cytosolic contents,at least change in kind and concentration of detergents for eliminate membrane debris were adjusted. All of the results step by step classified and optimized.Results: The optimized concentration of IPTG was 0.1 mM. There was not any significant difference between the used detergents as both of them had the same effect on permeabilization of the bacterial membranes. Finally we detected the RECOMBINANT GST-PEP by SDS page analysis with both of Commasie Brilliant Blue staining (CBB) and western blot using anti GST antibody.Conclusion: Taken together these data showed that PEP (peroxisomal PROTEIN)which containing fibronectin type III and two hydrophobic domains should be assessed by further proteomics analysis to discover it's interactions with other PROTEINs in neural stem differentiated cells.

Background: Shigellosis is a major global issue of human health. To date, no effective vaccine has been found against Shigella. One of the major virulent factors in Shigella dysenteriae type 1 is Shigella enterotoxin or STx. STxB has immunogenic, adjuvant, or carrier properties. Vaccine candidate antigens can be coupled with this adjuvant for production of an appropriate vaccine. IpaD has a key role in invasion, virulence, and infection by Shigella.Materials and Methods: In this study, the gene sequences of STXB and ipaD were obtained from gene bank and corresponding genes were prepared as synthetic construct and then transferred to E. coli BL21DE3. By PCR amplification and enzymatic digestion, PROTEIN expression levels were assessed. Its PROTEIN expression was confirmed by Western blot technique. After extraction by affinity chromatography, the RECOMBINANT PROTEIN was injected four times to guinea pigs. The pigs were, then, challenged by Shigella felexneri 2a and active toxin of E. coli O157: H7.Results: The results showed that groups of guinea pigs challenged with 28 ´LD50 of toxin completely survived. Furthermore, guinea pigs were challenged by inducing Shigella felexneri 2a in their eyes. The results showed that the control pigs got cataracts, whereas the immune pigs were in health.Conclusion: The findings of this study suggest that this RECOMBINANT PROTEIN is a good candidate for production of a RECOMBINANT vaccine against Shigella family.

Introduction: Globally, Salmonella enterica serotype Typhi is responsible for more than 10 million enteric fever cases, annually. Because of the emergence of multidrug resistance strains of many bacteria, including Salmonella Typhi, vaccination may be a preferred strategy to combat infectious diseases. In the present study, the efficiency of flagellin PROTEIN as a RECOMBINANT vaccine candidate was evaluated in BALB/c mice. Materials and Methods: For this aim, flagellin PROTEIN was expressed in E. coli BL21 (DE3). Mice were grouped into two groups: test and control. Test group were immunized by the intraperitoneal administration of RECOMBINANT PROTEIN in combination with Freund’ s adjuvant. Following the completion of the immunization period, the mice were challenged by IP injection of 10 LD50 of live Salmonella Typhi and subsequent culture of their spleens and livers. Results: Flagellin PROTEIN expression was confirmed by SDS-PAGE and Western blotting. ELISA showed the proper stimulation of the humoral immunity of the immunized mice. The bacterial count decreased significantly in the spleens and livers of the immunized animals in comparison to the control ones. Conclusions: Findings of this study show the efficiency of flagellin RECOMBINANT PROTEIN in protecting mice against Salmonella Typhi.