The 0.968[(K0.48Na0.52)]Nb0.95+xSb0.05O3-0.032(Bi0.5Na0.5)ZrO3 [KNNxS-BNZ] lead-free ceramics with nonstoichiometric niobium ion were fabricated via conventional solid-state sintering technique and their piezoelectric, dielectric and ferroelectric properties were investigated. When x= 0.010, enhanced piezoelectric properties (d33 ≈ 421 pC/N and kp ≈ 0.47) were obtained due to the construction of rhombohendral – tetragonal phase boundary near room temperature. The KNNxS-BNZ ceramics possesses enhanced Curie temperature (Tc) with improved piezoelectric constant. A large d33 of ~ 421 pC/N and a high Tc ~ 256 °C can be simultaneously induced in the ceramics with x= 0.010. Especially, good thermal stability was observed in a broad temperature range. The results indicated that our work could benefit development of KNN-based ceramics and widen their application range.

This article is protected by copyright. All rights reserved.

Properties and structures of nonstoichiometric (K, Na)NbO3-based lead-free ceramics

Phase transition and piezoelectric properties of dense (K0.48,Na0.52)0.95Li0.05SbxNb(1−x)O3-0.03Ca0.5(Bi0.5,Na0.5)0.5ZrO3 lead free ceramics

Defect engineering of high-performance potassium sodium niobate piezoelectric ceramics sintered in reducing atmosphere

KNN based high dielectric constant X9R ceramics with fine grain structure and energy storage ability

Composition dependence of phase structure and electrical properties in (0.98-x)K0.35Na0.65NbO3–0.02BaZrO3–xBi0.5Na0.5ZrO3 ternary ceramics

Structure and electrical properties of K0.5Na0.5Nb0.94−xSb0.06SnxO3 lead-free piezoelectric ceramics

https://doi.org/10.1016/j.psj.2022.102240

Host-derived bacillus spp. as probiotic additives for improved growth performance in broilers

Objective To prepare the specific monoclonal antibody (mAb) against E domain III (ED3) of duck Tembusu virus (DTMUV) and explore its neutralization activity. Methods The ED3 gene was amplified by using reverse transcription PCR according to the genome of the DTMUV AH-F10 strain. Then, the recombinant expression vector pET32a-ED3 was constructed and transformed into E.coli Rosetta. The ED3 protein was expressed and purified by nickel column affinity chromatography. After the recombinant ED3 protein was identified by SDS-PAGE and Western blot analysis, the BALB/c mice were immunized subcutaneously three times. The splenocytes of the immunized mice were hybridized with Sp2/0 myeloma cells, and the hybridization was screened by the limiting dilution method. The specificity and sensitivity of the antibody were identified by indirect immuno-fluorescent assay and Western blot analysis. Subsequently, antibody titers were determined by ELISA. Finally, this study titrated the neutralization titers of the antibodies on DTMUV-infected BHK-21 cells. Results The ED3 protein was successfully prepared and purified using the prokaryotic expression system. Three strains of monoclonal antibodies named B9D10C7, B9D7B8G10 and B9D7B8F11 were prepared. Their subtypes were IgG1, IgG2a and IgG2b, respectively. The titers of monoclonal antibody ascites can reach 1:51 200, and they could specifically recognize the E protein of DTMUV. Neutralization test showed that they had a certain neutralizing activities. Conclusion The monoclonal antibodies against ED3 protein of DTMUV are successfully prepared.

[Preparation of monoclonal antibody against E domain III (ED3) protein of duck Tembusu virus with neutralizing activity].

Objective Mice were immunized with purified virus inhibitory protein endoplasmic reticulum associated interferon inducible (viperin) to prepare polyclonal antibody and identify specificity. Methods BALB/c mice were injected with duck tembusu virus to generate viperin in mouse brain by intracranial injection. Viperin gene, cloned from mouse brain tissue by reverse transcription PCR, was inserted into pGEX-6p-1 prokaryotic expression vector and transformed into E. coli Rosetta. The recombinant viperin protein was induced by isopropyl thiogalactoside (IPTG) and its solubility was analyzed. The protein was purified by potassium chloride (KCl) staining and gel cutting method. Polyclonal antibody was prepared by immunizing mice with purified recombinant viperin protein subcutaneously through abdomen, and the titer of polyclonal antibody was determined by indirect ELISA. Western blot analysis and indirect fluorescence assay (IFA) were used to detect the transient expression of viperin protein in BHK-21 cells to identify the specificity and sensitivity of the prepared polyclonal antibody against viperin protein. Results The mouse viperin gene was successfully cloned and the viperin protein was expressed. The titer of the prepared anti-viperin polyclonal antibody reached 1:25 600. The mouse anti-viperin polyclonal antibody could specifically recognize the transient expression of viperin protein in BHK-21 cells. Conclusion Mouse polyclonal antibody against viperin protein with high specificity and sensitivity was successfully prepared.

[Preparation of mouse polyclonal antibodies against virus inhibitory protein endoplasmic reticulum associated interferon inducible (viperin)].

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Structure and electrical properties of K0.5Na0.5Nb0.94−xSb0.06SnxO3 lead-free piezoelectric ceramics

Host-derived bacillus spp. as probiotic additives for improved growth performance in broilers

[Preparation of monoclonal antibody against E domain III (ED3) protein of duck Tembusu virus with neutralizing activity].

[Preparation of mouse polyclonal antibodies against virus inhibitory protein endoplasmic reticulum associated interferon inducible (viperin)].