Search results for: Albumin, Bovine (BSA) HRP
#38394906 
2024/02/15
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A self-assembled 3D nanoflowers based nano-ELISA platform for the sensitive detection of pyridaben.
Biomimetic methods are invariably employed to synthesize hybrid organic-inorganic multilevel structure nanoflowers with self-assembly processes in aqueous solutions, which is an ideal way to meet the challenges of immobilizing antibodies or enzymes in nanomaterial based enzyme-linked immunosorbent assay (nano-ELISA). In this study, we developed protein-inorganic hybrid 3D nanoflowers composed of bovine serum albumin (BSA), horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG (IgG-HRP) and copper(Ⅱ) phosphate (BSA-(IgG-HRP)-Cu(PO)) using a self-assembly biomimetic method. The preparation process avoided the use of any organic solvent and protein immobilization did not require covalent modifications. Additionally, the unique hierarchical structure enhances the thermal and storage stability of HRP. The BSA-(IgG-HRP)-Cu(PO) hybrid 3D nanoflower was then applied to a nano-ELISA platform for pyridaben detection, achieving a 50% inhibition concentration of 3.90 ng mL. The nano-ELISA achieved excellent accuracy for pyridaben detection. Such a novel BSA-(IgG-HRP)-Cu(PO) hybrid 3D nanoflower provide an excellent reagent for small molecule immunoassay.He Chen, Li An, Meng Li, Hao Liu, Zhong Jin, Huan Ma, Jingwei Ma, Juan Zhou, Ran Duan, Di Zhang, Xiu Cao, Tieliang Wang, Xujin Wu
2705 related Products with: A self-assembled 3D nanoflowers based nano-ELISA platform for the sensitive detection of pyridaben.
96 tests96 tests96 tests100 ml100testsOne 96-Well Microplate Ki1 kitOne 96-Well Microplate Ki96TOne 96-Well Strip Micropl
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#38213962 2024/01/10
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Horseradish peroxidase-catalyzed polyacrylamide gels: monitoring their polymerization with BSA-stabilized gold nanoclusters and their functional validation in electrophoresis.
Polyacrylamide gel (PAG) is extensively used as a matrix for biomolecular analysis and fractionation. However, the traditional polymerization catalyst system ,,','-tetramethylethylenediamine (TEMED)/ammonium persulphate (APS) of PAG presents non-negligible toxicity. Herein, we utilized the green and efficient bio-enzyme horseradish peroxidase (HRP) to catalyze the gel polymerization of polyacrylamide. At the same time, the efficacy of this gel system in separating nucleic acids and proteins was confirmed by applying the gel system in electrophoresis. This study aims to explore a higher biosafety polyacrylamide gel polymerization catalytic system which can be applied to electrophoresis technology. Furthermore, in order to differentiate between the bio-enzymatic catalytic system and the traditional toxic catalytic system during polymerization, aggregation-induced luminescence (AIE) of bovine serum albumin-stabilized gold nanoclusters (BSA-Au NCs) was used to monitor the polymerization reaction of the system. The results indicated that the fluorescence intensity of the polymeric system containing BSA-Au NCs increased with the polymerization of the monomers. Subsequently, we assessed whether certain components of nucleic acid electrophoresis and protein electrophoresis such as sodiumdodecylsulfate (SDS) and TBE buffer (Tris-boric acid, EDTA, pH 8.3) would affect the polymerization of the polyacrylamide gels catalyzed by the biological enzymes. The experimental conditions were also optimized to explore the optimal concentration of the ternary system of HRP, HO and ACAC. Our results suggested that the bioenzyme-catalyzed system could be a feasible alternative to the TEMED/APS-catalyzed system, which also could provide new insights into the methods of monitoring the polymerization system.Chang Liao, Tao Li, Fengjiao Chen, Shaoying Yan, Liying Zhu, Hua Tang, Dan Wang
2562 related Products with: Horseradish peroxidase-catalyzed polyacrylamide gels: monitoring their polymerization with BSA-stabilized gold nanoclusters and their functional validation in electrophoresis.
8 ml 1 g 8 ml 100ug-100μg60 mg 1000 ml 1000 ml
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#38101285 2023/11/15
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Dual-functionalized two-dimensional metal-organic framework composite with highly hydrophilicity for effective enrichment of glycopeptides.
Protein glycosylation research is currently focused on the development of various functionalized materials that can effectively enrich the levels of glycopeptides in samples. However, most of these materials possess limited glycopeptide-specific recognition sites because of large steric hindrance, unsuitable mass transfer kinetics, and relatively low surface areas. Herein, a highly hydrophilic two-dimensional (2-D) metal-organic framework (MOF) nanosheet modified with glutathione (GSH) and l-cysteine (l-Cys) (denoted as Zr-Fc MOF@Au@GC) has been synthesized for efficient glycopeptide enrichment. Using this composite material, 39 and 44 glycopeptides from horseradish peroxidase (HRP) and human serum immunoglobulin G (IgG) digests were detected, respectively, which represents a higher efficiency for glycopeptide enrichment from model glycoprotein digests than has been previously reported. The material Zr-Fc MOF@Au@GC exhibited ultra-high sensitivity (0.1 fmol/µL), excellent selectivity (weight ratio of HRP tryptic digest to bovine serum albumin (BSA) tryptic digest = 1:2000), good binding capacity (200 mg/g), satisfactory reusability, and long-term storage capacity. In addition, 655 glycopeptides corresponding to 366 glycoproteins were identified from human serum samples. To the best of our knowledge, this is the largest number of glycoproteins detected in human serum samples to date. These results indicated that Zr-Fc MOF@Au@GC has the potential to be used for the enrichment of glycopeptides in biological samples and the analysis of protein glycosylation.Xiaoyu Yuan, Jiayi Song, Han Wang, Wenkang Zhang, Ying Liu, Ping Su, Yi Yang
1984 related Products with: Dual-functionalized two-dimensional metal-organic framework composite with highly hydrophilicity for effective enrichment of glycopeptides.
1.0 mg4 Membranes/Box 1 G2 Pieces/Box 2x5L100ug Lyophilized 5 G4 Arrays/Slide0.1 mg1 kit1 mg
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#37848166 2023/10/15
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Counterion optimization for hydrophobic ion pairing (HIP): Unraveling the key factors.
In the present study, various surfactants were combined with insulin (INS), bovine serum albumin (BSA) and horseradish peroxidase (HRP) via hydrophobic ion pairing to increase lipophilicity and facilitate incorporation into self-emulsifying drug delivery systems (SEDDS). Lipophilicity of model proteins was successfully increased, achieving log D values up to 3.5 (INS), 3.2 (BSA) and 1.2 (HRP). Hereby, key factors responsible for complex formation were identified. In particular, surfactants with branched alkyl chains or chain lengths greater than C12 showed favorable properties for hydrophobic ion pairs (HIP). Furthermore, flexibility of the carbon chain resulted in higher lipophilicity and suitability of polar head groups of surfactants for HIP decreased in the rank order sulfonate > sulfosuccinate > phosphate = sulfate > carbonate > phosphonic acids = sulfobetaines. Stability studies of formed HIP complexes were performed in various gastrointestinal fluids and their solubility was determined in commonly used SEDDS excipients. Formed complexes were stable in simulated gastrointestinal fluids and could be incorporated into SEDDS formulations (C1: 10% caprylocaproyl polyoxyl-8 glycerides, 20% PEG-40 hydrogenated castor oil, 20% medium-chain triglycerides, 50% n-butanol; C2: 10% caprylocaproyl polyoxyl-8 glycerides, 20% PEG-40 hydrogenated castor oil, 20% medium-chain triglycerides, 40% n-butanol, 10% 1,2-butanediol), resulting in suitable payloads of up to 11.9 mg/ml for INS, 1.0 mg/ml for BSA and 1.6 mg/ml for HRP.Victor Claus, Matthias Sandmeier, Nathalie Hock, Helen Spleis, Sera Lindner, Monika Kalb, Andreas Bernkop-Schnürch
1758 related Products with: Counterion optimization for hydrophobic ion pairing (HIP): Unraveling the key factors.
100 tests0.1mg 1 G 1Lmin 2 cartons500 MG250ul25 µg100.00 ul
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#37355354 2023/06/19
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Protein separation by sequential selective complex coacervation.
In food manufacturing and particular biomedical products selected proteins are often required. Obtaining the desired proteins in a pure form from natural resources is therefore important, but often very challenging. Herein, we design a sequential coacervation process that allows to efficiently isolate and purify proteins with different isoelectric points (pIs) from a mixed solution, namely Bovine Serum Albumin (BSA, pI = 4.9) and Peroxidase from Horseradish (HRP, pI = 7.2). The key to separation is introducing a suitable polyelectrolyte that causes selective complex coacervation at appropriate pH and ionic strength. Specifically, polyethyleneimine (PEI), when added into the mixture at pH 6.0, produces a coacervation which exclusively contains BSA, leading to a supernatant solution containing 100 % HRP with a purity of 91 %. After separating the dilute and dense phases, BSA is recovered by adding poly(acrylic acid) (PAA) to the concentrated phase, which displaces BSA from the complex because it interacts more strongly with PEI. The supernatant phase after this step contains approximately 75 % of the initial amount of BSA with a purity of 99 %. Our results confirm that coacervation under well-defined conditions can be selective, enabling separation of proteins with adequate purity. Therefore, the established approach demonstrates a facile and sustainable strategy with potential for protein separation at industrial scale.Jin Zhou, Ying Cai, Yuting Wan, Bohang Wu, Jinbo Liu, Xinxin Zhang, Weiwei Hu, Martien A Cohen Stuart, Junyou Wang
1359 related Products with: Protein separation by sequential selective complex coacervation.
1 mg100 0.5 ml1 Set1mg1mg5 ml501mg100ug
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#36926885 2023/03/16
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Polymerization-Induced Proteinosome Formation Initiated by Artificial Cells.
Cellular communication is essential for living cells to coordinate the individual cellular responses and make collective behaviors. In the past decade, the communications between artificial cells have aroused great interest due to the potential applications of the structures in bioscience and biotechnology. To mimic the cellular communication, artificial cell assisted synthesis of proteinosomes was studied in this research. Multienzyme proteinosomes with glucose oxidase (GOx) and horseradish peroxidase (HRP) decorated on the membranes were synthesized by the thermally triggered self-assembly approach. Free radicals produced in a cascade reaction taking place on the surfaces of the multienzyme proteinosomes initiated reversible addition-fragmentation chain transfer (RAFT) polymerization of NIPAM at a temperature above LCST of PNIPAM in the presence of bovine serum albumin (BSA) or alcohol dehydrogenase (ADH)/acetaldehyde dehydrogenase (ALDH), and daughter proteinosomes with BSA or ADH/ALDH on the surfaces were fabricated. The structures of the GOx/HRP initiator proteinosomes, and the synthesized daughter proteinosomes were characterized with transmission electron microscopy, atomic force microscopy, fluorescence microscopy, dynamic light scattering, and micro-DSC. Enzyme activity assays demonstrate the high bioactivities of the enzymes on the surfaces of the initiator and the synthesized daughter proteinosomes.Luyang Liu, Chen Wang, Fang Liu, Hanying Zhao
2935 related Products with: Polymerization-Induced Proteinosome Formation Initiated by Artificial Cells.
1.00 flask1.5x10(6) cells100ug1mg30ml250 1.00 flask96 tests 1 kit(s) 50ml1.00 flask
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#36897022 2023/03/10
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Phosphorylation of KRT8 (keratin 8) by excessive mechanical load-activated PKN (protein kinase N) impairs autophagosome initiation and contributes to disc degeneration.
Excessive mechanical load (overloading) is a well-documented pathogenetic factor for many mechano stress-induced pathologies, i.e. intervertebral disc degeneration (IDD). Under overloading, the balance between anabolism and catabolism within nucleus pulposus (NP) cells are badly thrown off, and NP cells undergo apoptosis. However, little is known about how the overloading is transduced to the NP cells and contributes to disc degeneration. The current study shows that conditional knockout of (keratin 8) within NP aggravates load-induced IDD in vivo, and overexpression of endows NP cells greater resistance to overloading-induced apoptosis and degeneration in vitro. Discovery-driven experiments shows that phosphorylation of KRT8 on Ser43 by overloading activated RHOA-PKN (protein kinase N) impedes trafficking of Golgi resident small GTPase RAB33B, suppresses the autophagosome initiation and contributes to IDD. Overexpression of and knockdown of and , at an early stage of IDD, ameliorates disc degeneration; yet only knockdown of and , when treated at late stage of IDD, shows a therapeutic effect. This study validates a protective role of during overloading-induced IDD and demonstrates that targeting overloading activation of PKNs could be a novel and effective approach to mechano stress-induced pathologies with a wider window of therapeutic opportunity. AAV: adeno-associated virus; AF: anulus fibrosus; ANOVA: analysis of variance; ATG: autophagy related; BSA: bovine serum albumin; cDNA: complementary deoxyribonucleic acid; CEP: cartilaginous endplates; CHX: cycloheximide; cKO: conditional knockout; Cor: coronal plane; CT: computed tomography; Cy: coccygeal vertebra; D: aspartic acid; DEG: differentially expressed gene; DHI: disc height index; DIBA: dot immunobinding assay; dUTP: 2'-deoxyuridine 5'-triphosphate; ECM: extracellular matrix; EDTA: ethylene diamine tetraacetic acid; ER: endoplasmic reticulum; FBS: fetal bovine serum; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GPS: group-based prediction system; GSEA: gene set enrichment analysis; GTP: guanosine triphosphate; HE: hematoxylin-eosin; HRP: horseradish peroxidase; IDD: intervertebral disc degeneration; IF: immunofluorescence staining; IL1: interleukin 1; IVD: intervertebral disc; KEGG: Kyoto encyclopedia of genes and genomes; KRT8: keratin 8; KD: knockdown; KO: knockout; L: lumbar vertebra; LBP: low back pain; LC/MS: liquid chromatograph mass spectrometer; LSI: mouse lumbar instability model; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MMP3: matrix metallopeptidase 3; MRI: nuclear magnetic resonance imaging; NC: negative control; NP: nucleus pulposus; PBS: phosphate-buffered saline; PE: p-phycoerythrin; PFA: paraformaldehyde; PI: propidium iodide; PKN: protein kinase N; OE: overexpression; PTM: post translational modification; PVDF: polyvinylidene fluoride; qPCR: quantitative reverse-transcriptase polymerase chain reaction; RHOA: ras homolog family member A; RIPA: radio immunoprecipitation assay; RNA: ribonucleic acid; ROS: reactive oxygen species; RT: room temperature; TCM: rat tail compression-induced IDD model; TCS: mouse tail suturing compressive model; S: serine; Sag: sagittal plane; SD rats: Sprague-Dawley rats; shRNA: short hairpin RNA; siRNA: small interfering RNA; SOFG: safranin O-fast green; SQSTM1: sequestosome 1; TUNEL: terminal deoxynucleotidyl transferase dUTP nick end labeling; VG/ml: viral genomes per milliliter; WCL: whole cell lysate.Di Wang, Qiliang Shang, Jianxin Mao, Chu Gao, Jie Wang, Dong Wang, Han Wang, Haoruo Jia, Pandi Peng, Mu Du, Zhuojing Luo, Liu Yang
2880 related Products with: Phosphorylation of KRT8 (keratin 8) by excessive mechanical load-activated PKN (protein kinase N) impairs autophagosome initiation and contributes to disc degeneration.
1 Set1 Set1 Set50 1 Set200IU1 Set1 Set1 Set100ug1 Set1 Set
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#36832055 2023/02/17
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Horseradish Peroxidase-Encapsulated Fluorescent Bio-Nanoparticle for Ultra-Sensitive and Easy Detection of Hydrogen Peroxide.
Hydrogen peroxide (HO) has been a fascinating target in various chemical, biological, clinical, and industrial fields. Several types of fluorescent protein-stabilized gold nanoclusters (protein-AuNCs) have been developed for sensitive and easy detection of HO. However, its low sensitivity makes is difficult to measure negligible concentrations of HO. Therefore, to overcome this limitation, we developed a horseradish peroxidase-encapsulated fluorescent bio-nanoparticle (HEFBNP), comprising bovine serum albumin-stabilized gold nanoclusters (BSA-AuNCs) and horseradish peroxidase-stabilized gold nanoclusters (HRP-AuNCs). The fabricated HEFBNP can sensitively detect HO owing to its two properties. The first is that HEFBNPs have a continuous two-step fluorescence quenching mechanism, which comes from the heterogenous fluorescence quenching mechanism of HRP-AuNCs and BSA-AuNCs. Second, the proximity of two protein-AuNCs in a single HEFBNP allows a reaction intermediate (•OH) to rapidly reach the adjacent protein-AuNCs. As a result, HEFBNP can improve the overall reaction event and decrease the loss of intermediate in the solution. Due to the continuous quenching mechanism and effective reaction event, a HEFBNP-based sensing system can measure very low concentrations of HO up to 0.5 nM and show good selectivity. Furthermore, we design a glass-based microfluidic device to make it easier use HEFBNP, which allowed us to detect HO with the naked eye. Overall, the proposed HO sensing system is expected to be an easy and highly sensitive on-site detection tool in chemistry, biology, clinics, and industry fields.Myeong-Jun Lee, Ji-Ae Song, Jin-Ha Choi, Jeong-Hyeop Shin, Ji-Woon Myeong, Ki-Ppeum Lee, Taehwan Kim, Ki-Eob Park, Byung-Keun Oh