Structural and thermodynamic study of Ca A- or Co B-site substituted SrFeO3-δ perovskites for low temperature chemical looping applications.
»
Structural and thermodynamic study of Ca A- or Co B-site substituted SrFeO3-δ perovskites for low temperature chemical looping applications.
Perovskite-structured materials, because the chemical-physical properties and composition tuneable, have expanded their range of applications for the chemical looping process, in which the lattice oxygen supply of oxygen required for the chemical reaction to eliminate the use of co-feeding oxidant gas.
To optimize the behavior of oxygen donate them for specific applications a fundamental understanding of the characteristics of the reduction / oxidation of perovskite structured oxides and their manipulation through the introduction of dopants is key. In this study, we investigate the nature of the desorption / absorption of structural and oxygen from SR1-xCaxFeO3-δ and SrFe1-xCoxO3-δ (0 ≤ x ≤ 1) to guide the design of more effective oxygen carriers for chemical looping applications at low temperature (ie 400- 600 ° C). Ca A- or B-site co-delta replaced SrFeO3 show reducibility increases, so that a higher oxygen capacity at T ≤ 600 ° C when compared to samples substituted.
Quantitative assessment of the thermodynamic properties (partial molar enthalpy and entropy of vacancy formation) confirms the reduced formation enthalpy of a vacancy on the substitution in the temperature range (ie, 400-600 ° C). Among the samples tested, Sr0.8Ca0.2FeO3-δ exhibited the highest oxygen storage capacity (2.15 wt%) at 500 ° C, equipped with a redox excellent and the structural stability of more than 100 cycles. Rate thermodynamics, supported by in situ XRD measurements revealed that the release of oxygen occurs in the transition phase of perovskite-brownmillerite below 770 ° C, while the perovskite structure remains stable above 770 ° C.
Structural and thermodynamic study of Ca A- or Co B-site substituted SrFeO3-δ perovskites for low temperature chemical looping applications.
Chemical Modifications in RNA Interference and CRISPR / Cas Genome Editing Reagents.
chemically modified oligonucleotides (ONS) are routinely used in the laboratory to assess gene function, and clinical progress fast forward as the continuous efforts undertaken to optimize the efficacy ON. For years, RNA interference (RNAi) has become one of the main tools used to inhibit RNA expression in various species.
Attempts have been made to improve the administration of exogenous double-stranded RNA component by intracellular endogenous RNAi machinery to direct degradation of the target RNA efficacious user defined. More recently, synthetic RNA ons used to replicate system CRISPR / Cas-derived bacteria specific to directly edit the mammalian genome. Both of these techniques rely on the use of various chemical modification to RNA phosphate backbone or sugar in certain positions throughout ons to enhance the desired biological outcome.
Relevant chemical modifications also include a targeting ligand conjugated to help ON delivery to specific cell types. chemical modification that is most beneficial for ounce therapies that are relevant, because they serve to enhance the binding targets, increased longevity drugs, facilitating the targeting cell-specific, increasing internalization into the compartment intracellular productive, and reduces both sequence-specific and related to the immune target effects (OTES).
Description: SAE1 Antibody: Small ubiquitin-like modifiers (SUMOs) are a family of small, related proteins (SUMO-1/2/3/4) that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation, a major regulator of protein function in cellular processes such as nuclear transport, transcriptional regulation, apoptosis and protein stability. This sumoylation is effected by the heterodimeric enzyme SAE1/SAE2 and the SUMO-1-conjugating enzyme Ubch9. The sumoylation pathway mediated by SAE1/SAE2 is distinct from other ubiquitin-like protein (Ubl) pathways.
Description: A polyclonal antibody against SAE1. Recognizes SAE1 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:2000-1:5000, WB:1:500-1:2000, IHC:1:25-1:100
Description: A polyclonal antibody against SAE1. Recognizes SAE1 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:2000-1:5000, WB:1:500-1:2000, IHC:1:15-1:50
Description: A polyclonal antibody against SAE1. Recognizes SAE1 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IF;WB:1:500-1:3000, IF:1:100-1:500
Description: A polyclonal antibody against SAE1. Recognizes SAE1 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC; Recommended dilution: IHC:1:20-1:200
Description: A polyclonal antibody against SAE1. Recognizes SAE1 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB
Description: A polyclonal antibody against SAE1. Recognizes SAE1 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: WB, IHC, IF, ELISA;WB:1/500-1/2000.IHC:1/100-1/300.IF:1/200-1/1000.ELISA:1/20000
Description: A polyclonal antibody against SAE1. Recognizes SAE1 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IF;WB:1:500-1:3000, IF:1:100-1:500
Description: A polyclonal antibody for detection of SAE1 from Human, Mouse, Rat. This SAE1 antibody is for WB, IHC-P, IF, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human SAE1 at AA range: 190-270
Description: A polyclonal antibody for detection of SAE1 from Human, Mouse, Rat. This SAE1 antibody is for WB, IHC-P, IF, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human SAE1 at AA range: 190-270
Description: A polyclonal antibody for detection of SAE1 from Human, Mouse, Rat. This SAE1 antibody is for WB, IHC-P, IF, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human SAE1 at AA range: 190-270
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human SAE1 . This antibody is tested and proven to work in the following applications:
Description: Description of target: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.
This subsection of the ‘Function’ section describes the metabolic pathway(s) associated with a protein.
Description: Description of target: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.
This subsection of the ‘Function’ section describes the metabolic pathway(s) associated with a protein.
Description: Description of target: Posttranslational modification of proteins by the addition of the small protein SUMO (see SUMO1, MIM 601912), or sumoylation, regulates protein structure and intracellular localization. SAE1 and UBA2 (MIM 613295) form a heterodimer that functions as a SUMO-activating enzyme for the sumoylation of proteins (Okuma et al., 1999 [PubMed 9920803]).[supplied by OMIM, Mar 2010];Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.078 ng/mL
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human SAE1 (AOS1) (C-term). This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody raised in Goat that recognizes and binds to Human Goat Anti-SAE1 / AOS1 . This antibody is tested and proven to work in the following applications:
Description: A Monoclonal antibody against Human SAE1 (clone 1G8). The antibodies are raised in Mouse and are from clone 1G8. This antibody is applicable in WB and IHC-P, IF
Description: A Monoclonal antibody against Human SAE1 (monoclonal) (M01). The antibodies are raised in Mouse and are from clone 1G4-1G5. This antibody is applicable in WB, IHC and IF, E
Description: SAE1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids (1-346 a.a.) and having a molecular mass of 42.2 kDa. The SAE1 is fused to 32 amino acid T7-Tag at N-terminus and purified by proprietary chromatographic techniques. _x000D_
SAE1 sgRNA CRISPR/Cas9 All-in-One Lentivector set (Human)
The knowledge gained from years of RNAi reagents to optimize and characterize the properties of biochemistry and biophysics of any chemical modifications will hopefully speed up the CRISPR / Cas technology to the clinic, as well as expanding the use of RNAi to treat the disease when undruggable. This review discusses the most common chemical modification used in RNAi reagents and CRISPR / Cas RNA guide and provide an overview of select publications that have shown success in improving ON efficacy and / or reduce unwanted OTES.
