Search results for: Albumin, Egg 〔Ovalbumin〕
#28890022 2017/09/11 Save this To Up
Lymphoproliferative responses to dendritic cell presentation of sensitizing allergens in atopic children with multiple allergies.Peripheral blood mononuclear cells (PBMCs) proliferate inconsistently, rendering current lymphoproliferation assays unreliable in diagnosis.
1732 related Products with: Lymphoproliferative responses to dendritic cell presentation of sensitizing allergens in atopic children with multiple allergies.Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri Nycodenz, non ionic, non Rat Anti-Mouse Dendritic Multiple lung carcinoma ( Oral squamous cell cancer anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl CELLKINES Natural Human I CELLKINES INTERLEUKIN 2 ( CELLKINES INTERLEUKIN 2 (
#28734606 2017/07/23 Save this To Up
Thiol-yne click synthesis of boronic acid functionalized silica nanoparticle-graphene oxide composites for highly selective enrichment of glycoproteins.In this work, a facile novel strategy is developed for the preparation of 4-mercapto-phenylboronic acid functionalized silica nanoparticle-graphene oxide composite (GO@MPBA) via thiol-yne click reaction. The morphology, structure and composition of the resulting GO@MPBA was characterized by transmission electron microscopy, X-ray powder diffraction, Fourier transform infrared spectroscopy, Fourier transform Raman spectroscopy, Thermogravimetric analysis and X-ray photoelectron spectrometry. GO@MPBA exhibited the high binding capacity towards glycoproteins such as ovalbumin (1288.8mgg(-1)), immunoglobulin G (1144.1mgg(-1)), transferrin (592.1mgg(-1)) and horseradish peroxidase (392.4mgg(-1)), in contrast, the binding capacity of each non-glycoproteins (cytochrome c, deoxyribonuclease A, pepsin, trypsin, lysozyme and bovine serum albumin) is less than 50mgg(-1). Furthermore, the GO@MPBA still remained a good binding capacity after the five times of adsorption-desorption cycles. The selective enrichment of glycoproteins from real egg white samples by GO@MPBA was demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. This work could present a facile novel approach of surface modification to design environmentally friendly and more efficient adsorbents for the isolation and enrichment of glycoprotein from complex biological samples.
2880 related Products with: Thiol-yne click synthesis of boronic acid functionalized silica nanoparticle-graphene oxide composites for highly selective enrichment of glycoproteins.2 Formylfuran 5 boronic a (5Z)-7-[(5-Acetyloxy-2-fo (5Z)-7-[(5-Acetyloxy-2-fo B-(6-Amino-2-pyridinyl)bo 2-Aminopyrimidine-5-boron 3-Formylindol-1-yl-acetic Quinoline 8 boronic acid 8 Octadecyloxypyrene 1,3, 4 Formylphenylboronic aci 5 (4 Formyl 3,5 dimethoxy 8 Octanoyloxypyrene 1,3,6 2-Methylquinoline-6-boron
#28493685 2017/05/11 Save this To Up
Selective Detection of Shiga-like Toxin 1 from Complex Samples Using Pigeon Ovalbumin Functionalized Gold Nanoparticles as Affinity Probes.Escherichia coli O157:H7 is a foodborne pathogen. This bacterial strain can generate Shiga-like toxins (SLTs), which can cause serious sickness and even death. Thus, it is important to develop effective and sensitive methods that can be used to rapidly identify the presence of SLTs from complex samples. Pigeon egg white (PEW) contains abundant glycoproteins, including pigeon ovalbumin (POA) (∼60%). POA possesses Gal-α(1→4)-Gal-β(1→4)-GlcNAc termini, which can recognize the B subunits in SLT type 1 (SLT-1B). Thus, POA is a suitable probe for trapping SLT-1B. In this work, we used PEW proteins as starting materials to react with aqueous tetrachloroauric acid for generation of PEW-protein-immobilized gold nanoparticles (AuNPs@PEW) via one-pot reactions. We demonstrated that the generated AuNPs@PEW were mainly dominated by POA-immobilized Au NPs. The as-prepared AuNPs@PEW were used as affinity probes to selectively probe SLT-1B from complex cell lysates derived from E. coli O157:H7. The selective trapping step can be completed within ∼90 s under microwave heating (power = 450 W) to enrich sufficient SLT-1B for matrix-assisted laser desorption/ionization (MALDI) mass spectrometric analysis. Furthermore, this approach can be used to detect SLT-1B at a concentration as low as ∼40 pM. The feasibility of using the proposed method to selectively detect SLT-1B from ham contaminated by E. coli O157:H7 was also demonstrated.
1677 related Products with: Selective Detection of Shiga-like Toxin 1 from Complex Samples Using Pigeon Ovalbumin Functionalized Gold Nanoparticles as Affinity Probes.MiRNA Northern Blot Assay Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M PiColorlock Gold Tankyrase 1 Colorimetric Tankyrase 1 Chemiluminesc Rabbit Anti-Shiga-like to Rabbit Anti-ASM Acid sphi Rabbit Anti-D.Aspartic ac Rabbit Anti-ASB7 Polyclon Rabbit Anti-ASB17 Polyclo QuantiChrom™ Acetylchol
#28449993 2017/04/28 Save this To Up
In vitro peptic digestion of ovomucin-depleted egg white affected by pH, temperature and pulsed electric fields.The effect of pH (4, 5, 7, and 9) combined with either heat (60, 80°C for 10min) or pulsed electric fields (PEF) (1.4-1.8kV/cm, 260-690kJ/kg) treatments on the in vitro peptic digestion of ovomucin-depleted egg white was investigated. Protein digestibility, unaffected by 60°C heating, was increased by heating at 80°C, which caused protein aggregation and solution turbidity. Compared to ovalbumin and lysozyme, ovotransferrin was more susceptible to pepsinolysis. Susceptibility to pepsinolysis of ovalbumin and lysozyme was markedly enhanced by heating at 80°C, compared to either 60°C heating or PEF processing. MALDI-MS identified proteolytic fragments from ovalbumin and lysozyme, exhibiting varied resistance to pepsinolysis. PEF processing at ∼690kJ/kg and pH 4 increased protein digestibility to a similar level to that obtained after heating at 80°C, with negligible solution turbidity, showing potential for the production of digestible protein drinks with good consumer visual appeal owing to their clarity.
1152 related Products with: In vitro peptic digestion of ovomucin-depleted egg white affected by pH, temperature and pulsed electric fields.Caspase-3 Inhibitor Q-DEV Caspase-3 Inhibitor Q-DEV Caspase-3 Inhibitor Q-DEV ATM Kinase Inhibitor, KU- Elastase Inhibitor, SPCK; FAAH Inhibitor, PF-622; A FAAH Inhibitor, PF-622; A GSK-3 Inhibitor, AR-A0144 GSK-3 Inhibitor, AR-A0144 DPP IV Inhibitor, NVP DPP DPP IV Inhibitor, NVP DPP Myeloperoxidase Inhibitor
#28434227 2017/04/24 Save this To Up
How Proteins Aggregate Can Reduce Allergenicity: Comparison of Ovalbumins Heated under Opposite Electrostatic Conditions.Heated foods are recommended for avoiding sensitization to food proteins, but depending on the physicochemical conditions during heating, more or less unfolded proteins aggregate differently. Whether the aggregation process could modulate allergenicity was investigated. Heating ovalbumin in opposite electrostatic conditions led to small (A-s, about 50 nm) and large (A-L, about 65 μm) aggregates that were used to sensitize mice. The symptoms upon oral challenge and rat basophil leukemia degranulation with native ovalbumin differed on the basis of which aggregates were used during the sensitization. Immunoglobulin-E (IgE) production was significantly lower with A-s than with A-L. Although two common linear IgE-epitopes were found, the aggregates bound and cross-linked IgE similarly or differently, depending on the sensitizing aggregate. The ovalbumin aggregates thus displayed a lower allergenic potential when formed under repulsive rather than nonrepulsive electrostatic conditions. This further demonstrates that food structure modulates the immune response during the sensitization phase with some effects on the elicitation phase of an allergic reaction and argues for the need to characterize the aggregation state of allergens.
2406 related Products with: How Proteins Aggregate Can Reduce Allergenicity: Comparison of Ovalbumins Heated under Opposite Electrostatic Conditions.Native Canine CASQ2 Prote Native Canine CASQ2 Prote Native Canine CASQ2 Prote Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C Sheep Anti-Canine Urokina Hidensity ovarian cancer CA125, Ovarian Cancer An
#28394320 2017/04/10 Save this To Up
Angiotensin-converting enzyme affects the presentation of MHC class II antigens.Antigen processing and presentation through the MHC class II pathway is critical for activating T helper cells. Angiotensin-converting enzyme (ACE) is a carboxyl peptidase expressed by antigen-presenting cells. By analysis of ACE null (knockout), wild-type, and ACE-overexpressing (ACE10) mice and the antigen-presenting cells derived from these mice, we found that ACE has a physiological role in the processing of peptides for MHC class II presentation. The efficiency of presenting MHC class II epitopes from ovalbumin (OVA) and hen egg lysosome is markedly affected by cellular ACE levels. Mice overexpressing ACE in myeloid cells have a much more vigorous CD4(+) T-cell and antibody response when immunized with OVA. ACE is present in the endosomal pathway where MHC class II peptide processing and loading occur. The efficiency of MHC class II antigen presentation can be altered by ACE overexpression or ACE pharmacological inhibition. Thus, ACE is a dynamic participant in processing MHC class II peptides. Manipulation of ACE expression by antigen-presenting cells may prove to be a novel strategy to alter the immune response.
1546 related Products with: Angiotensin-converting enzyme affects the presentation of MHC class II antigens.Mouse Anti-Mouse MHC Clas Rat Anti-Rat MHC Class II Mouse Anti-Rat MHC Class Mouse Anti-Rat MHC Class Mouse Anti-Rat MHC Class Mouse Anti-Rat MHC Class Mouse Anti-Rat MHC Class Mouse Anti-Rat MHC Class Mouse Anti-Rat MHC Class Mouse Anti-Rat MHC Class Mouse Anti-Rat MHC Class Mouse Anti-Rat MHC Class
#28273492 2017/03/08 Save this To Up
Enhanced ovalbumin stability at oil-water interface by phosphorylation and identification of phosphorylation site using MALDI-TOF mass spectrometry.To improve the interfacial properties, a phosphorylation modification of OVA was performed through dry-heating at three different pH values (5.0, 7.0 and 9.0) in the presence of sodium tripolyphosphate. X-ray photoelectron and Raman spectroscopies confirmed that phosphate groups were successfully grafted onto the ovalbumin backbone through covalent interaction to form OP bond. Additionally, 23, 21 and 18 phosphorylation sites were identified in the OVA that had been phosphorylated at pH 5.0, 7.0 and 9.0 (P-OVA5, P-OVA7 and P-OVA9) respectively by MALDI-TOF mass spectroscopy. More phosphorylated peptides and possible phosphorylation sites were found here than in previous studies with the reaction time reduced to 12h. As a result, the iso-electric point (pI) of P-OVA shifted to lower pH, improving the stability of the P-OVA-included system over a wider pH range. The dynamic interfacial tension, which depends on the phosphorylation-induced conformational change, was explored by Fourier-transform Raman and circular dichroism spectroscopies, and the equilibrium interfacial tension decreased from 17.359mNm(-1) for natural OVA (N-OVA) to 15.969mNm(-1) for P-OVA9. Furthermore, P-OVA was applied to O/W emulsions, resulting in a narrower size distribution with a smaller particle size in P-OVA-stabilized emulsions than in N-OVA-stabilized emulsions. The increase rate of mean particle diameter after 60-min storage decreased from 72.37% for N-OVA to 7.97% for P-OVA5, implying a significant improvement of emulsion stability by preventing aggregation and coalescence. The results from this work demonstrated that the natural biopolymer can be applied to O/W emulsions by enhancing interfacial properties with phosphorylation.
1763 related Products with: Enhanced ovalbumin stability at oil-water interface by phosphorylation and identification of phosphorylation site using MALDI-TOF mass spectrometry.SMCC Plus™ *Enhanced wa ATM(phospho S1981) & ATM ATXN1(phospho T236) & ATX ATF2(phospho S62 S44) & A ATF2(phospho T69 T51) & A ATF2(phospho T71 T53) & A ATF2(phospho T73 T55) & A ATF2(phospho S112 S94) & ATF4(phospho S245) & ATF4 ATM(phospho S1981) & ATM ATF2(Phospho T51) & ATF2 ATF2(Phospho S322) & ATF2
#28234975 2017/02/24 Save this To Up
Critical role of intestinal interleukin-4 modulating regulatory T cells for desensitization, tolerance, and inflammation of food allergy.The mechanism inducing either inflammation or tolerance to orally administered food allergens remains unclear. To investigate this we analyzed mouse models of food allergy (OVA23-3) and tolerance (DO11.10 [D10]), both of which express ovalbumin (OVA)-specific T-cell receptors.
1287 related Products with: Critical role of intestinal interleukin-4 modulating regulatory T cells for desensitization, tolerance, and inflammation of food allergy.GLP 2 ELISA Kit, Rat Prog Breast invasive ductal ca 5 Formyl 2 thiopheneboron Formylmethyl triphenylpho Interleukin-34 IL34 (N-t HLTV I envelope recombina Anti C Reactive Protein A Anti VGLUT 1 Rat, polyclo MOUSE ANTI BOVINE ROTAVIR Anti Rat VGLUT 2, Rabbit Epidermal Growth Factor ( Epidermal Growth Factor (
#28231415 2017/02/23 Save this To Up
Encapsulating an Immunosuppressant Enhances Tolerance Induction by Siglec-Engaging Tolerogenic Liposomes.Unwanted antibody responses significantly impact human health, and current options for treating deleterious antibody responses largely rely on broad immunosuppressants that can compromise overall immunity. A desirable alternative is to induce antigen-specific immune tolerance. We have shown that co-presentation of antigen and ligands of B cell sialic acid-binding immunoglobulin-like lectins (Siglecs) on a liposomal nanoparticle induces antigen-specific tolerance. Although Siglec-engaging tolerance-inducing antigenic liposomes (STALs) induce robust B cell tolerance in naïve mice, the full potential of STALs requires long-term tolerance induction and suppression of an ongoing immune response. We hypothesized that STALs encapsulated with rapamycin (RAPA), an immunomodulator, could improve the efficacy of STALs and potentially enable their use in the context of immunological memory. Here, we showed that formulation of STALs with RAPA produced enhanced tolerance induction in naïve mice compared to STALs without RAPA but had minimal impact on inducing tolerance in previously sensitized mice. These findings indicate that the addition of immunomodulators to STALs could be beneficial in tolerance induction and support future development of STALs for the treatment of allergy and autoimmune diseases.
1250 related Products with: Encapsulating an Immunosuppressant Enhances Tolerance Induction by Siglec-Engaging Tolerogenic Liposomes.Rabbit Anti-CD328 Siglec- Mouse anti human Siglec-3 Mouse anti human Siglec-5 Mouse anti human Siglec-1 Mouse anti human Siglec-7 Mouse anti human Siglec-9 Rat monoclonal anti mouse B-Phycoerythrin antibody 2-Amino Benzimidazole Su 2-Amino Benzimidazole Su EZH2 KMT6 Control Peptid EZH2 KMT6 antibody Isoty
#28215692 2017/02/20 Save this To Up
Developing a puncture-free in ovo chicken transfection strategy based on bypassing albumen nucleases.Chicken is a dual-purpose animal important from both agricultural and medical aspects. Even though significant improvements have been made in chicken transgenesis technologies, chicken genome manipulation has not been widely used in developmental biology. This study was aimed to evaluate chicken egg white nuclease properties and thereof plausibility of devising an in vivo transfection technology without causing physical damage to the embryo. First, the nuclease activity of egg albumen was assessed. The egg white nucleases were strongly active in degrading DNA and RNA. The egg white DNase activity was comparable to commercially available DNase-I. Nuclease activities were also assessed after heating, proteinase K, or EDTA treatment. Unlike proteinase K, both heating and EDTA were noticeably effective for the nuclease inactivation. Simultaneous application of lipoplex form of DNA (1 μg pDB2: 3 μl Lipofectamine2000) and EDTA showed a synergistic effect in protection against egg white nucleases. Finally, we injected the lipoplexes with or without EDTA close to the embryo at day0, but outside the embryonic epiblast. Implementation of a scrutinized PCR assay indicated that transfection took place only when EDTA was complemented to the lipoplexes. The transfection rate of day4 embryos and the hatched chicks were 54.5 and 30.0%, respectively. EGFP expression was detected in two out of three transgenic chicks. In conclusion, this study provided a detail analysis of chicken egg albumen nuclease properties and suggested the feasibility of developing a puncture-free handmade technology for transfection of the chicken embryo.
2319 related Products with: Developing a puncture-free in ovo chicken transfection strategy based on bypassing albumen nucleases.Mouse Anti-Chicken Interl Internexin NF66 Antibody, Rabbit Anti-intestinal FA Rabbit Anti-FGF3 Oncogene Rat Anti-Mouse Interleuki Chicken Anti-Influenza HA Chicken antiBovine Insuli Interleukins Recombinant Interleukin-34 IL34 (N-t Interleukin-34 IL34 anti Fatty acid free heat sho Fatty acid free heat sho
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