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Search results for: Anti Albumin produced in rabbit

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#32994501   2020/09/29 To Up

Neo-antigens for the serological diagnosis of IgE-mediated drug allergic reactions to antibiotics cephalosporin, carbapenem and monobactam.

New antigens deriving from -lloyl and -llanyl, major and minor determinants, respectively, were produced for β-lactam antibiotics cefuroxime, cefotaxime, ceftriaxone, meropenem and aztreonam. Twenty β-lactam antigens were produced using human serum albumin and histone H1 as carrier proteins. Antigens were tested by multiplex in vitro immunoassays and evaluated based on the detection of specific IgG and IgE in the serum samples. Both major and minor determinants were appropriate antigens for detecting specific anti-β-lactam IgG in immunised rabbit sera. In a cohort of 37 allergic patients, we observed that only the minor determinants (-llanyl antigens) were suitable for determining specific anti-β-lactam IgE antibodies with high sensitivity (< 0.01 IU/mL; 24 ng/L) and specificity (100%). These findings reveal that not only the haptenisation of β-lactam antibiotics renders improved molecular recognition events when the 4-member β-lactam ring remains unmodified, but also may contribute to develop promising minor antigens suitable for detecting specific IgE-mediated allergic reactions. This will facilitate the development of sensitive and selective multiplexed in vitro tests for drug-allergy diagnoses to antibiotics cephalosporin, carbapenem and monobactam.
Edurne Peña-Mendizabal, Sergi Morais, Ángel Maquieira

2001 related Products with: Neo-antigens for the serological diagnosis of IgE-mediated drug allergic reactions to antibiotics cephalosporin, carbapenem and monobactam.

500 reactions100 reactions100 Reactions400 reactions 1 module500 mg100 ug 100 reactions 

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#32485925   2020/05/29 To Up

Immunization with Bovine Serum Albumin (BSA) in Oil-Adjuvant Elicits IgM Antibody Response in Chinese Soft-Shelled Turtle ().

Immunoassays are among the frontline methods used for disease diagnosis and surveillance. Despite this, there are no immunoassays developed for the Chinese soft-shelled turtle (), which has expanded into large scale commercial production in several Asian countries. One of the critical factors delaying the development of immunoassays is the lack of characterized soft-shelled turtle immunoglobulins. Herein, we used mass spectrometry together with the ProtQuest software to identify the soft-shelled turtle IgM heavy chain in serum, which again was used to produce a polyclonal anti-turtle-IgM in rabbits. Thereafter, the polyclonal anti-turtle-IgM was used as a secondary antibody in an indirect ELISA to evaluate antibody responses of soft-shelled turtles injected with the bovine serum albumin (BSA) model antigen. Our findings show that only turtle immunized with a water-in-oil BSA plus ISA 763A VG adjuvant (SEPPIC, France) emulsion had antibodies detected at 42 days post vaccination (dpv) while turtles injected with phosphate buffered saline (PBS) only as well as turtle injected with BSA dissolved in PBS had no significant antibody levels detected in serum throughout the study period. In summary, our findings show that rabbit polyclonal anti-turtle-IgM produced can be used in ELISA to measure serum antibody responses in immunized soft-shelled turtles. Future studies should explore its application in other immunoassays needed for the disease diagnosis and vaccine development for soft-shelled turtles.
Cheng Xu, Jiehao Xu, Yu Chen, Øystein Evensen, Hetron Mweemba Munang'andu, Guoying Qian

1809 related Products with: Immunization with Bovine Serum Albumin (BSA) in Oil-Adjuvant Elicits IgM Antibody Response in Chinese Soft-Shelled Turtle ().

100ug200ul10 ml100 ml100 ml50ul50 ml50 ml100 μg500 ml96T100 ml

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#31583234   2019/08/06 To Up

Production of a polyclonal antibody against acrylamide for immunochromatographic detection of acrylamide using strip tests.

To produce, purify, and characterize a polyclonal antibody against acrylamide (anti-AA) for an application to immunochromatographic strip tests for AA.
Lusiani Dewi Assaat, Endang Saepudin, Retno Damayanti Soejoedono, Rahmat Setya Adji, Okti Nadia Poetri, Tribidasari Anggraningrum Ivandini

1812 related Products with: Production of a polyclonal antibody against acrylamide for immunochromatographic detection of acrylamide using strip tests.

96 tests500 tests100 TESTS96 tests0.1 ml500 tests100ug Lyophilized100ug100ug Lyophilized100ug Lyophilized100ug Lyophilized

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#30861576   2019/03/12 To Up

Comparison of indirect peroxidase and avidin-biotin-peroxidase complex (ABC) immunohistochemical staining procedures for c-fos in rat brain.

c-Fos is the product of a gene expressed within neurons in the brain that serves as an anatomical marker of cellular activation. Immunohistochemical staining for c-fos allows a characterization of the effects of many different types of experimental manipulations on neuronal activity, making it a powerful technique for understanding brain, drug and behavior relationships. This study compared visualization of an anti-c-fos primary antibody in 40-μm-thick cryostat sections of formaldehyde-fixed rat brainstem using either a peroxidase enzyme-conjugated secondary antibody (indirect peroxidase) or the peroxidase-conjugated avidin-biotin complex (ABC) method. All sections were treated with H O to quench endogenous peroxidase enzyme and sodium borohydride to enhance permeability of the tissue and improve staining quality. Every other section was used to examine either the indirect peroxidase or the ABC method. Sections for the indirect peroxidase method were treated with Triton X-100 detergent to increase tissue permeability, goat serum to reduce non-specific binding of the secondary antibody and, in some cases, bovine serum albumin (BSA) to reduce non-specific binding of the primary antibody. Sections for the ABC method were treated with dilute normal serum, and avidin and biotin solutions and, in some cases BSA. Alternate sections were incubated for 72 h in either rabbit anti-c-fos primary antibody (1 : 20 000) or its vehicle (negative control). For the indirect peroxidase protocol, tissues were treated with peroxidase-conjugated goat anti-rabbit secondary antibody. For the ABC protocol, tissues were treated with biotinylated goat anti-rabbit secondary antibody and ABC peroxidase complex. All sections were reacted with 3,3'-diaminobenzadine (DAB) and H O , mounted and coverslipped. Both methods produced specific staining of c-fos-containing neurons, relative to the negative control sections. The indirect peroxidase protocol produced clear staining of c-fos-containing neurons, with very little background in the negative control sections. Staining for c-fos was enhanced using the ABC method in that c-fos stained neurons were darker and more clearly visible after shorter treatment with DAB. However, negative control sections showed a greater amount of non-specific staining with the ABC method. Thus, the ABC method was more sensitive but showed reduced specificity, with BSA treatment slightly reducing the level of non-specific staining. Overall, the ABC method produced better visualization and contrast of c-fos-containing neurons against the background color of the tissue.
Jae L Butler, Beverly J Barham, Byron A Heidenreich

1126 related Products with: Comparison of indirect peroxidase and avidin-biotin-peroxidase complex (ABC) immunohistochemical staining procedures for c-fos in rat brain.

1 kit100ul100 μg100ug100ul100 μg100ug100ul100μg100μg100ul96/kit

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#30612650   2018/10/21 To Up

Ultrasensitive immunosensor for acrylamide based on chitosan/SnO-SiC hollow sphere nanochains/gold nanomaterial as signal amplification.

An electrochemical immunosensor for ultrasensitive detection of acrylamide (AA) in water and food samples was developed. SnO-SiC hollow sphere nanochains with high surface area and gold nanoparticles with good electroconductivity were fabricated onto the surface of a glassy carbon electrode pre-coated with chitosan. The coating antigen (AA-4-mercaptophenylacetic acid-ovalbumin conjugate, AA-4-MPA-OVA) was immobilized on the electrode. Polyclonal antibody specific for AA-4-MPA was conjugated to gold nanorod (AuNR) as primary antibody (AuNR-Ab). Horseradish peroxidase labelled anti-rabbit antibody produced in goat was conjugated to AuNR as secondary antibody (HRP-AuNR-Ab). For detection, the analyte (AA-4-MPA) in sample competed with coating antigen for binding with AuNR-Ab. After washing, HRP-AuNR-Ab was added to capture the AuNR-Ab, and the electrical signal was obtained by addition of hydroquinone and HO. After investigation of the binding ability on nanomaterials and optimization of competitive immunoassay conditions, the proposed immunosensor exhibited a sensitive response to AA with a detection limit of 45.9 ± 2.7 ng kg, and working range of 187 ± 12.3 ng kg to 104 ± 8.2 μg kg for drinking water samples. Recoveries of AA from spiked samples were ranged from 86.0% to 115.0%. The specificity, repeatability and stability of the immunosensor were also proved to be acceptable, indicating its potential application in AA monitoring.
Min-Fu Wu, Yu Wang, Sha Li, Xiu-Xiu Dong, Jin-Yi Yang, Yu-Dong Shen, Hong Wang, Yuan-Ming Sun, Hong-Tao Lei, Zhen-Lin Xu

2544 related Products with: Ultrasensitive immunosensor for acrylamide based on chitosan/SnO-SiC hollow sphere nanochains/gold nanomaterial as signal amplification.

500 tests96 Tests1 Bag of 1000 Caps/Unit x100tests50 assays1,000 tests100ug Lyophilized100Tests

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#30424519   2018/11/12 To Up

Generation of Highly Efficient Equine-Derived Antibodies for Post-Exposure Treatment of Ricin Intoxications by Vaccination with Monomerized Ricin.

Ricin, a highly lethal toxin derived from the seeds of (castor beans) is considered a potential biological threat agent due to its high availability, ease of production, and to the lack of any approved medical countermeasure against ricin exposures. To date, the use of neutralizing antibodies is the most promising post-exposure treatment for ricin intoxication. The aim of this work was to generate anti-ricin antitoxin that confers high level post-exposure protection against ricin challenge. Due to safety issues regarding the usage of ricin holotoxin as an antigen, we generated an inactivated toxin that would reduce health risks for both the immunizer and the immunized animal. To this end, a monomerized ricin antigen was constructed by reducing highly purified ricin to its monomeric constituents. Preliminary immunizing experiments in rabbits indicated that this monomerized antigen is as effective as the native toxin in terms of neutralizing antibody elicitation and protection of mice against lethal ricin challenges. Characterization of the monomerized antigen demonstrated that the irreversibly detached A and B subunits retain catalytic and lectin activity, respectively, implying that the monomerization process did not significantly affect their overall structure. Toxicity studies revealed that the monomerized ricin displayed a 250-fold decreased activity in a cell culture-based functionality test, while clinical signs were undetectable in mice injected with this antigen. Immunization of a horse with the monomerized toxin was highly effective in elicitation of high titers of neutralizing antibodies. Due to the increased potential of IgG-derived adverse events, anti-ricin F(ab')₂ antitoxin was produced. The F(ab')₂-based antitoxin conferred high protection to intranasally ricin-intoxicated mice; ~60% and ~34% survival, when administered 24 and 48 h post exposure to a lethal dose, respectively. In line with the enhanced protection, anti-inflammatory and anti-edematous effects were measured in the antitoxin treated mice, in comparison to mice that were intoxicated but not treated. Accordingly, this anti-ricin preparation is an excellent candidate for post exposure treatment of ricin intoxications.
Reut Falach, Anita Sapoznikov, Ron Alcalay, Moshe Aftalion, Sharon Ehrlich, Arik Makovitzki, Avi Agami, Avishai Mimran, Amir Rosner, Tamar Sabo, Chanoch Kronman, Yoav Gal

2520 related Products with: Generation of Highly Efficient Equine-Derived Antibodies for Post-Exposure Treatment of Ricin Intoxications by Vaccination with Monomerized Ricin.

1 mg1 mg1 mg4 Arrays/Slide 5 G4 Membranes/Box2 Pieces/Box4 Membranes/Box2 Pieces/Box4 Arrays/Slide2 Pieces/Box2 ml

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#29607560   2018/04/01 To Up

Intrauterine vaccination induces a dose-sensitive primary humoral response with limited evidence of recall potential.

Induction of the local mucosal immune system within the reproductive tract is widely considered to be a key component in the development of effective prophylactic vaccines to control the spread of sexually transmitted infections. Here, we examine the capacity of the upper reproductive tract to act as a site of immune induction following.
Jonathan Alexander Pasternak, Glenn Hamonic, Jill Van Kessel, Colette L Wheler, Michael K Dyck, Heather L Wilson

1444 related Products with: Intrauterine vaccination induces a dose-sensitive primary humoral response with limited evidence of recall potential.

100ug100ug100ug1 kit100ug100ug100ug100ug100ug100ug100ug100ug

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#29175317   2017/11/22 To Up

Epitope identification of specific naturally occurring human anti-avidin antibodies.

Human serum contains natural antibodies against avidin. Affinity purified natural anti-avidin human IgG exhibits affinity constants comparable to those of antibodies produced by active immunization of rabbits. Using a random hexapeptide library displayed on the filamentous M13 phage, and rabbit anti-avidin purified antibodies as a selector, we searched for epitopes shared by both selector and natural human anti-avidin IgG. This approach, enabled the isolation and identification of phagotopes bearing consensus motifs similar to sequence stretches of the avidin loops and β-sheet regions. These phagotopes were recognized by the natural human anti-avidin antibodies. The fact that natural anti-avidin antibodies in human serum have similar epitopes to those of IgG elicited by active immunization of animals, led us to suggest that small peptide epitopes may prevent deleterious effects caused by antibodies formed against food proteins as well as therapeutic proteins.
Boris Tchernychev, Talia Miron, Meir Wilchek

2854 related Products with: Epitope identification of specific naturally occurring human anti-avidin antibodies.

0.5 mg0.5 mg0.5 mg0.5 mg0.5 mg0.5 mg0.5 mg0.5 mg0.5 mg0.5 mg

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#28212503   2017/02/14 To Up

Lactobacillus buchneri S-layer as carrier for an Ara h 2-derived peptide for peanut allergen-specific immunotherapy.

Peanut allergy is an IgE-mediated severe hypersensitivity disorder. The lack of a treatment of this potentially fatal allergy has led to intensive research on vaccine development. Here, we describe the design and initial characterization of a carrier-bound peptide derived from the most potent peanut allergen, Ara h 2, as a candidate vaccine. Based on the adjuvant capability of bacterial surface (S-) layers, a fusion protein of the S-layer protein SlpB from Lactobacillus buchneri CD034 and the Ara h 2-derived peptide AH3a42 was produced. This peptide comprised immunodominant B-cell epitopes as well as one T cell epitope. The fusion protein SlpB-AH3a42 was expressed in E. coli, purified, and tested for its IgE binding capacity as well as for its ability to activate sensitized rat basophil leukemia (RBL) cells. The capacity of Ara h 2-specific IgG rabbit-antibodies raised against SlpB-AH3a42 or Ara h 2 to inhibit IgE-binding was determined by ELISA inhibition assays using sera of peanut allergic patients sensitized to Ara h 2. IgE specific to the SlpB-AH3a42 fusion protein was detected in 69% (25 of 36) of the sera. Despite the recognition by IgE, the SlpB-AH3a42 fusion protein was unable to induce β-hexosaminidase release from sensitized RBL cells at concentrations up to 100ng per ml. The inhibition of IgE-binding to the natural allergen observed after pre-incubation of the 20 sera with rabbit anti-SlpB-AH3a42 IgG was more than 30% for four sera, more than 20% for eight sera, and below 10% for eight sera. In comparison, anti-Ara h 2 rabbit IgG antibodies inhibited binding to Ara h 2 by 48% ±13.5%. Our data provide evidence for the feasibility of this novel approach towards the development of a peanut allergen peptide-based carrier-bound vaccine. Our experiments further indicate that more than one allergen-peptide will be needed to induce a broader protection of patients allergic to Ara h 2.
Julia Anzengruber, Merima Bublin, Eva Bönisch, Bettina Janesch, Angelika Tscheppe, Matthias L Braun, Eva-Maria Varga, Christine Hafner, Heimo Breiteneder, Christina Schäffer

1416 related Products with: Lactobacillus buchneri S-layer as carrier for an Ara h 2-derived peptide for peanut allergen-specific immunotherapy.

0.2 mg25 µg1 ml0.1 ml0.25 mg25 µg100 TESTS0.2 mg1 LITRE 100ul96 Tests100 ml

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#28101473   2016/12/22 To Up

Purification and Characterization of Bovine Serum Albumin Using Chromatographic Method.

Albumin is an abundant protein of blood and has many biopharmaceutical applications. The aim of this study was to purify bovine serum albumin (BSA) using produced rabbit anti-BSA antibody. The polyclonal antibody was produced against the BSA in rabbits. Then, the pure BSA was injected to three white New Zealand rabbits. ELISA test was done to evaluate antibody production. After antibody purification,the purified antibody was attached to CNBr-activated sepharose and finally it was used for purification of albumin from bovine serum. Western blotting analysis was used for functional assessment of immunoaffinity purified BSA. The titer of anti-bovine albumin determined by ELISA was obtained 1: 256000. The SDS-PAGE showed up to 98% purity of isolated BSA and western blotting confirmed the BSA functionality. Purified bovine serum albumin by affinity chromatography showed a single band with molecular weight of 66 KDa. Affinity chromatography using produced rabbit anti-BSA antibody would be an economical and safe method for purification of BSA.
Sanaz Balkani, Sara Shamekhi, Ramin Raoufinia, Reza Parvan, Jalal Abdolalizadeh

2389 related Products with: Purification and Characterization of Bovine Serum Albumin Using Chromatographic Method.

100ug50ul100 μg100ug1 ml50ul200ul100ug100ul1 ml200ul100ug

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