Log In Sign up
The largest database of trusted experimental protocols
> Chemicals & Drugs > Amino Acid > Immunoglobulin A

Immunoglobulin A

Immunoglobulin A (IgA) is a class of antibodies that play a crucial role in the mucosal immune system.
IgA is the predominant immunoglobulin found in secretions such as saliva, tears, and mucus, where it helps protect the body against pathogens and allergens.
It is also present in the blood and other bodily fluids.
IgA can exist in monomeric, dimeric, and secretory forms, each with distinct functionalities.
Resaerch on IgA is important for understading the mucosal immune response, as well as its invovlement in various diseases and conditions.
PubCompare.ai can help optimize your IgA research by providing access to protocols from literature, preprints, and patents, and leveraging AI-driven comparisons to identify the best protocols and products for your studies.

Most cited protocols related to «Immunoglobulin A»

1
Correlates of HIV-1 Infection Risk in RV144 Vaccine Trial
Cited 65 times
The correlates study was preceded by pilot studies from November 2009 through July 201120 (Fig. S1 in the Supplementary Appendix, available with the full text of this article at NEJM.org). Pilot assays were performed on samples taken at baseline and week 26 from 50 to 100 uninfected RV144 participants (80% of whom were vaccine recipients and 20% of whom were placebo recipients) and scored according to four statistical criteria: a low false positive rate on the basis of samples from placebo and vaccine recipients at baseline, a large dynamic range of vaccine-induced immune responses, nonredundancy of responses (low correlations), and high reproducibility.
Of the 32 types of antibody, T-cell, and innate immunity assays evaluated in pilot studies, 17 met these criteria, from which 6 primary variables were chosen for assessment as correlates of infection risk. The purpose was to restrict the primary analysis to a limited number of variables in order to optimize the statistical power for showing a correlation of risk between vaccinated persons who acquired versus those who did not acquire HIV-1. The primary variables included 5 Env-specific antibody responses and 1 cellular response: the binding of plasma IgA antibodies to Env, the avidity of IgG antibodies for Env, antibody-dependent cellular cytotoxicity, HIV-1 neutralizing antibodies, the binding of IgG antibodies to variable regions 1 and 2 (V1V2) of the gp120 Env, and the level of Env-specific CD4+ T cells (for details, see the Supplementary Appendix). All 17 types of immune assays and their 152 component variables were also included in the secondary correlates analyses (Tables S1 and S2 in the Supplementary Appendix).
Secondary variables were drawn from the remaining 152 assays selected from pilot assay studies; they were evaluated to help interpret the results of the primary analysis and to generate additional hypotheses (Table S1 in the Supplementary Appendix). For the sensitivity analysis, immune-response variables that were closely related to the six primary variables (within the same assay type) were substituted for each of the primary variables into the multivariable model (eight variables, with three individual variables paired to the primary variable of neutralizing antibodies) (Table S2 in the Supplementary Appendix). All assays were performed by personnel who were unaware of treatment assignments and case–control status.
Haynes B.F., Gilbert P.B., McElrath M.J., Zolla-Pazner S., Tomaras G.D., Alam S.M., Evans D.T., Montefiori D.C., Karnasuta C., Sutthent R., Liao H.X., DeVico A.L., Lewis G.K., Williams C., Pinter A., Fong Y., Janes H., DeCamp A., Huang Y., Rao M., Billings E., Karasavvas N., Robb M.L., Ngauy V., de Souza M.S., Paris R., Ferrari G., Bailer R.T., Soderberg K.A., Andrews C., Berman P.W., Frahm N., De Rosa S.C., Alpert M.D., Yates N.L., Shen X., Koup R.A., Pitisuttithum P., Kaewkungwal J., Nitayaphan S., Rerks-Ngarm S., Michael N.L, & Kim J.H. (2012). Immune-Correlates Analysis of an HIV-1 Vaccine Efficacy Trial. The New England Journal of Medicine, 366(14), 1275-1286.
Publication 2012
Antibodies, Neutralizing Antibody Avidity Antibody Formation Biological Assay CD4 Positive T Lymphocytes Cells Cytotoxicities, Antibody-Dependent Cell HIV-1 HIV Antibodies HIV Envelope Protein gp120 Hypersensitivity Immunity, Innate Immunoglobulin A Immunoglobulin G Immunoglobulins Infection Placebos Plasma Response, Immune T-Lymphocyte Vaccines
2
Novel Diagnostic Approaches for Celiac Disease
Cited 31 times
While the current standard tests of serology and conventional histology are usually adequate to reach a diagnosis of CD, there are patients whose tests are equivocal and diagnostic uncertainty remains. Several novel diagnostic approaches have been undertaken. The deposition of IgA antibodies in close proximity to TG2 in the small intestine has shown promise as a way of defining early or potential CD in patients who are seropositive but lack any of the usual histological markers for CD. Recent work from Finland on IgA-TG2 autoantibody deposition in the small intestine in such patients shows promise in delivery of an early prediction of development of CD. However, this is currently experimental and the methodology requires tissue sections frozen in liquid nitrogen.124 (link) Another diagnostic method meriting further evaluation is EmA assay in the culture medium of small intestinal biopsies.125 (link)
126 (link) Other investigators have reported their findings using new techniques associated with endoscopy to enhance the diagnosis of CD. These include confocal microscopy, high-resolution magnification endoscopy, optical band imaging127 (link) and optimal coherence tomography. These novel techniques are still limited by availability, tolerability and cost.98 (link) However, the immersion technique and dye enhancement in which the endoscopist instills water or a contrast dye (for example, indigo carmine or methylene blue) into the bowel lumen, with or without the assistance of magnification endoscopy, enhancing the visualisation of the villus128 (link) can be readily used and improves visualisation of villi, thus increasing the sensitivity for detection of villous atrophy.98 (link)
Ludvigsson J.F., Bai J.C., Biagi F., Card T.R., Ciacci C., Ciclitira P.J., Green P.H., Hadjivassiliou M., Holdoway A., van Heel D.A., Kaukinen K., Leffler D.A., Leonard J.N., Lundin K.E., McGough N., Davidson M., Murray J.A., Swift G.L., Walker M.M., Zingone F, & Sanders D.S. (2014). Diagnosis and management of adult coeliac disease: guidelines from the British Society of Gastroenterology. Gut, 63(8), 1210-1228.
Publication 2014
Atrophy Autoantibodies Biological Assay Biopsy Culture Media Diagnosis Endoscopy Freezing Hypersensitivity Immunoglobulin A Indigo Carmine Intestines Intestines, Small Methylene Blue Microscopy, Confocal Nitrogen Obstetric Delivery Patients Submersion Tests, Serologic Tissues Tomography Vision
3
Dengue Virus Infection Diagnosis
Cited 22 times
An acute case is considered positive for dengue if 1) dengue virus (DENV) is isolated in C6/36 Ae. albopictus cells (11 (link)) and serotyped by RT-PCR (12 (link)), 2) DENV RNA is detected by RT-PCR (12 (link), 13 (link)) after extraction from serum samples by using the QIAamp Viral RNA Mini Kit (Qiagen, Valencia, California), 3) seroconversion is demonstrated by using acute and convalescent paired sera by a DENV-specific immunoglobulin M capture enzyme-linked immunosorbent assay (14 (link)), and/or 4) antibody titer by inhibition enzyme-linked immunosorbent assay (2 (link), 15 (link)) demonstrates a 4-fold or greater increase in titer in paired acute and convalescent sera as calculated by using the Reed-Muench method (16 ). Those whose paired annual samples demonstrate seroconversion or an increase in DENV-specific antibody titer during the year, but who have not had an identifiable febrile episode associated with acute DENV infection, are considered “inapparent DENV infections.”
Kuan G., Gordon A., Avilés W., Ortega O., Hammond S.N., Elizondo D., Nuñez A., Coloma J., Balmaseda A, & Harris E. (2009). The Nicaraguan Pediatric Dengue Cohort Study: Study Design, Methods, Use of Information Technology, and Extension to Other Infectious Diseases. American Journal of Epidemiology, 170(1), 120-129.
Publication 2009
Cells Dengue Fever Dengue Virus Enzyme-Linked Immunosorbent Assay Fever Immunoglobulin A Immunoglobulins Psychological Inhibition Reverse Transcriptase Polymerase Chain Reaction RNA, Viral Serum
4
Dengue and JEV Antibody Capture ELISA
Cited 16 times
When Innis and coworkers described the IgM capture ELISA for dengue in 1989, they included JEV antigens to differentiate dengue and JEV infections [4 (link)]. This detail is important in settings where both dengue and JEV co-circulate and we have adapted this basic assay to utilize culture supernatants instead of mouse brain derived antigens and monoclonal instead of polyclonal antibodies. We validated the use of culture supernatants as the antigen source previously [5 (link)] and the current assay uses in addition an equal mixture of the monoclonal antibodies MF4/5/A5/C3-3/D4/C6 and MV12/1/C2-2/1, which together can recognize all 4 dengue serotypes as well as JEV. Table 2 shows adjusted OD readings of a mouse immunoglobulin capture ELISA (MIC ELISA) to show the specificities of these 2 monoclonal antibodies. Thus MF4/5/A5/C3-3/D4/C6 is a dengue group reactive antibody and MV12/1/C2-2/1 is JEV specific.
Briefly, 96 well flat bottom plates (Maxisorb, Nunc, Denmark) were coated overnight at 4°C with rabbit anti-human μ chain (Dako A425) at 1:2000 dilution in carbonate-bicarbonate buffer pH 9.6 before blocking with PBS containing 1% casein. Washed plates were loaded with patients serum (in triplicate) at 1:100 dilution in PBS containing 1% casein and incubated at room temperature for 2 hours before washing with PBS containing 0.5% Tween 20 (PBS-Tween). Each specimen was then tested against 3 different antigens: DENV pool (of all 4 serotypes), JEV and the uninfected cell control. These antigens were loaded into the wells for an overnight incubation at 4°C and then washed with PBS-Tween prior to the antigen detection step, which uses a mixture of the monoclonal antibodies MF4/5/A5/C3-3/D4/C6 and MV12/1/C2-2/1 for one hour at room temperature. After washing with PBS-Tween the bound monoclonals were detected using an anti-mouse immunoglobulin conjugated with HRP (Dako P260) at 1:2000 dilution for one hour at room temperature. Colour development was achieved after washing using the substrate, o-phenylenediamine – hydrogen peroxide for 30 minutes at room temperature. The reaction was stopped with sulphuric acid and the optical density (OD) was read at 490 nm wavelength using 650 nm as the reference.
Cardosa M.J., Wang S.M., Sum M.S, & Tio P.H. (2002). Antibodies against prM protein distinguish between previous infection with dengue and Japanese encephalitis viruses.. BMC Microbiology, 2, 9.
Publication 2002
1,2-diaminobenzene Antibodies, Anti-Idiotypic Antibody Specificity Antigens Biological Assay Brain Buffers Carbonates Caseins Cells Dengue Fever Enzyme-Linked Immunosorbent Assay Homo sapiens Immunoglobulin A Immunoglobulins Infection Ion, Bicarbonate Monoclonal Antibodies Mus Patients Peroxide, Hydrogen Rabbits Serum Sulfuric Acids Technique, Dilution Tween 20 Tweens Vision
5
Seroprevalence Study Protocol for COVID-19 Surveillance
Cited 12 times
An example of the full study flow is outlined in Fig. 3. Informed written or electronic consent is obtained before any procedure of the study visit. Participants can fill the baseline questionnaire online or use a paper form. The questionnaire takes approximately 20 min to complete and includes demographic questions, symptoms, other tests taken for SARS-CoV-2, preventative measure behaviors, and quality of life measures. Details of the questions asked of the participants are given in Table 3. The full questionnaires used nationwide are published in the online supplementary material.

Example study flow of seroprevalence studies (Corona Immunitas, Switzerland, 2020–2021)

Example of schedule of assessments (Corona Immunitas, Switzerland, 2020–2021)

ContactsInvitation/recruitmentStudy visit (BL)Digital follow-up
TimingPrior to Day 0Day 0Week 1 to week 52 (weekly)
Study invitationX
Invitation for Baseline data collection (and visit—depending on center)X
Confirmation letter or email, written informationX

Baseline questionnaire (online):

 Personal demographics & health data

 COVID-19 specific data; including symptoms, hospitalization, relevant medications, other SARS-CoV-2 tests

 Socio-demographic data

 Economic impact due to lockdown measures

 Persons in immediate vicinity and their relevant symptoms

 Preventive measures, exposure and level of concern over pandemic

XX
Oral and/or written informationX
Check inclusion-/ exclusion criteriaX
Written consentX
Blood samplingX
Information on test interpretationX
Information on digital follow-upX
Information on further procedure according to subpopulationX

Weekly digital follow-up questionnaire (online):

Symptoms, healthcare professional contacts, hospitalizations, test results, preventive measures

X

Monthly digital follow-up questionnaire (online):

 Access to health care, behavior, daily activities, mental health, well-being, usage of SwissCovid App (FOPH 2020d ), motivation to participate in study

X

BL baseline

Venous blood sampling is performed at a blood collection site or at home. All staff have access to the necessary infrastructure for blood withdrawal and safe storage of biological samples. The entire process follows Standardized Operating Procedures (SOPs). Blood drawing is performed by trained healthcare staff (i.e., nurse, assistant nurse, or junior doctor). The quantity of blood varies according to the study site, and depending on whether additional analyses are performed. Standard hygiene rules are followed such as usual handwashing, disinfection procedures, and wearing of masks and gloves. All participants are required to wear a mask, provided by the study team, during all interactions.
Samples are transported to a local laboratory or the Vaud Central University Hospital (CHUV) directly or centrifuged before transport to the laboratory if possible, aliquoted and stored in a biobank on each site at − 20 °C or − 80 °C before the serological test. Samples are delivered within 16 h of being taken. Team members are trained in safe management practices and procedures for contamination accidents. Serum is prepared with serum gel and plasma with ethylenediaminetetraacetic acid (EDTA) before the serology test. Depending on the site, serum or plasma from the drawn venous blood is analyzed for the presence of SARS-CoV-2 IgG and IgA antibodies. Some study sites will store additional serum, saliva or plasma samples in a biobank for further use in this or in other studies; genetic and epigenetic analyses are planned in several centers. Participants are informed about the planned analyses and provide broad consent for future research use of biospecimens.
The study data are collected and managed using REDCap electronic data capturing tools (Harris et al. 2019 (link)) hosted at the responsible universities. Websites of study centers are fully detailed in the supplementary material Table S1.
West E.A., Anker D., Amati R., Richard A., Wisniak A., Butty A., Albanese E., Bochud M., Chiolero A., Crivelli L., Cullati S., d’Acremont V., Epure A.M., Fehr J., Flahault A., Fornerod L., Frank I., Frei A., Michel G., Gonseth S., Guessous I., Imboden M., Kahlert C.R., Kaufmann L., Kohler P., Mösli N., Paris D., Probst-Hensch N., Rodondi N., Stringhini S., Vermes T., Vollrath F, & Puhan M.A. (2020). Corona Immunitas: study protocol of a nationwide program of SARS-CoV-2 seroprevalence and seroepidemiologic studies in Switzerland. International Journal of Public Health, 65(9), 1529-1548.
Full text: Click here
Publication 2020
Accidents Biopharmaceuticals BLOOD Childbirth COVID 19 Disease Management Disinfection Edetic Acid Fingers Health Personnel Hospitalization Immunoglobulin A Mental Health Motivation Nurses Pharmaceutical Preparations Physicians, Junior Plasma Saliva SARS-CoV-2 Serum Tests, Serologic Veins

Most recents protocols related to «Immunoglobulin A»

1
ELISA Detection of Serum IgG and IgA Antibodies
Serum IgG and IgA antibodies were measured by an ELISA in-house protocol. Briefly, 96 well microtiter plates (Corning) were coated with 5 µg/mL of SF2a LPS (extracted from SF2a 454) in carbonate buffer for 1 h at 37 °C. Unbound sites were blocked with 150 µl of blocking buffer containing 0.5% bovine serum albumin (BSA) (Merck Millipore Corp.) and 0.5% Casein for 1 h at 37 °C. Wells were washed twice (PBS Tween) and duplicates of tested samples were serially 2-fold diluted (initial dilution 1:200) in blocking buffer, added to the wells and incubated overnight (ON) at room temperature (RT). Plates were washed four times and 100 µl/well of alkaline phosphatase (AP) conjugated anti-human IgG or IgA (KPL, Inc. USA) was added and incubated ON at RT. Wells were washed four times and 100 µl/well of phosphatase substrate, para-nitrophenyl phosphate (pNPP) one component (SouthernBiotech) was added and plates were incubated in the dark for 15 min at RT. The reaction was stopped by the addition of 50 µl/well of Stop solution (3 M NaOH). Absorbance was measured at 405 nm using an ELISA plate reader (Multiskan FC, Thermo Scientific). Results were expressed in endpoint titers (the last serum dilution yielding an optical density (O.D.) of 0.2 or higher).
Meron-Sudai S., Asato V., Adler A., Bialik A., Goren S., Ariel-Cohen O., Reizis A., Mulard L.A., Phalipon A, & Cohen D. (2023). A Shigella flexneri 2a synthetic glycan-based vaccine induces a long-lasting immune response in adults. NPJ Vaccines, 8, 35.
Full text: Click here
Publication 2023
4-aminophenylphosphate 4-nitrophenyl Alkaline Phosphatase anti-IgG Carbonates Cardiac Arrest Caseins Enzyme-Linked Immunosorbent Assay Homo sapiens Immunoglobulin A Phosphates Phosphoric Monoester Hydrolases Serum Serum Albumin, Bovine Technique, Dilution Tweens
2
Egg Quality and Immunity in Hens
Several moderator variables were used to baseline information. Inclusion criteria
included moderator variables [study location, breed, treatment duration, age of
hens, number of hens used in the study, carotenoid (source, level, and form)
added to feed], as well as mean value, SD, and SE. The parameters observed were
egg quality [egg weight, shell thickness, egg yolk color, Haugh unit (HU), egg
yolk cholesterol (EYC), egg yolk carotenoids], performance (feed consumption,
FCR, final body weight, egg production), and immunity [immunoglobulin A (IgA)
and white blood cells (WBC)].
Yunitasari F., Jayanegara A, & Ulupi N. (2023). Performance, Egg Quality, and Immunity of Laying Hens due to Natural Carotenoid Supplementation: A Meta-Analysis. Food Science of Animal Resources, 43(2), 282-304.
Publication 2023
Body Weight Carotenoids Cholesterol Immunoglobulin A Response, Immune Yolks, Egg
3
Lung Viral Titers and Antibody Response
Mice were sacrificed at 2 and 4 days p.i., lungs were collected and snap frozen for preparing the lung homogenates for viral titer measurement according to our previous publication60 . Mice were sacrificed at 15 days p.i., and whole blood was collected through the posterior vena cava vein. Serum was separated from whole blood by centrifugation (12,000 × g, 10 min at room temperature). The IAV-specific IgG2a and IgA antibodies in serum were determined using ELISA via serial dilution as described in our previous publication60 .
Wang Q., Sundar I.K., Lucas J.H., Park J.G., Nogales A., Martinez-Sobrido L, & Rahman I. (2023). Circadian clock molecule REV-ERBα regulates lung fibrotic progression through collagen stabilization. Nature Communications, 14, 1295.
Full text: Click here
Publication 2023
BLOOD Centrifugation Enzyme-Linked Immunosorbent Assay Freezing IgG2A Immunoglobulin A Lung Mice, House Serum Technique, Dilution Veins Vena Cavas, Inferior
4
Chicken Blood Analysis Protocol
At the end of the study period (12th week), 24 birds [six birds from each group (1 per replicate)] were selected for sample collection after 12 h fasting. About 5 ml of blood were collected from the jugular veins, then kept in a micro-anticoagulant tube in slanting position for 30 min, centrifuged at 1,500 x g for 15 min (Tang et al., 2017 (link)). The harvested plasma was transferred to Eppendorf tubes (1.5 ml) and stored at –20°C until analysis. The whole blood samples were put together in an ice pack and transported to the laboratory for hematology analysis within 1 h of collection. For hematological indices analysis, an automated hematology analyzer (Model: BC-2800 Vet, Mindray, Shenzhen, China) was used. Red blood cell indices, MCH, MCV and mean cell hemoglobin concentration (MCHC), were calculated (Jain, 1993 ).
Before analysis of biochemical indices, the serum was thawed at 4°C and kept at low temperature during the whole process in order to avoid activation of enzymes. Determination of glutathione peroxidase (GST), glutathione peroxidase (GSH-Px), total antioxidant capacity (T-AOC), total superoxide dismutase (T-SOD), catalase (CAT), and malondialdehyde (MDA) were achieved using an assay kits from ML Bio and Jiancheng Bioengineering Institute (Nanjing, China), and measured spectrophotometrically (Shimadzu, model UV-1800, Tokyo, Japan). Serum concentrations of immunoglobulins A (IgA), immunoglobulins G (IgG), immunoglobulins M (IgM) and complement proteins; C3 and C4 were determined with the corresponding chicken ELISA kits. All standards were tested in duplicate and concentrations of IgA, IgG, IgM, C3, and C4 were determined using standard curves constructed from the standards run on the plate. All the ELISA kits adopted in the study are of high specificity and sensitivity for chickens, and all procedures were done according to the manufacturer’s instructions.
Obianwuna U.E., Qiu K., Wang J., Zhang H.J., Qi G.H., Huang L.L, & Wu S.G. (2023). Effects of dietary Clostridium butyricum and fructooligosaccharides, alone or in combination, on performance, egg quality, amino acid digestibility, jejunal morphology, immune function, and antioxidant capacity of laying hens. Frontiers in Microbiology, 14, 1125897.
Full text: Click here
Publication 2023
Anticoagulants Antioxidants Aves Biological Assay BLOOD Catalase Chickens Cold Temperature Complement System Proteins DNA Replication Enzyme-Linked Immunosorbent Assay Enzyme Activation Erythrocyte Indices Hypersensitivity Immunoglobulin A Immunoglobulin G Immunoglobulin M Jugular Vein Malondialdehyde Mean Cell Hemoglobin Concentration Peroxidase, Glutathione Plasma Serum Specimen Collection Superoxide Dismutase
5
Optimized Bovine Protein Database for Mass Spectrometry
Cited 1 time
For optimal results, and overcoming the limitations of incomplete, poorly annotated and highly redundant bovine protein databases, a customized protein database was created for the searches. The one protein sequence per gene version of the Bos taurus (taxon ID 9913) reference proteome (ID UP000009136) of 8 January 2022 was downloaded from UniProt (https://www.uniprot.org/proteomes/UP000009136) in FASTA format on 3 March 2022. This database was further processed by removing residual duplicate sequences (i.e. protein sequences with the same gene name), adding complete sequence where only fragment sequences were present, and updating the FASTA headers to the current headers of the date of download, i.e. 3 March 2022. Considering that the bovine immunoglobulins in UniProt were listed under the names “uncharacterized protein” or “Ig domain-containing protein”, functional bovine immunoglobulin heavy and light chain, constant and variable sequences were downloaded from the reference directory of the international ImMunoGeneTics information system (IMGT RefSeq, https://www.imgt.org/vquest/refseqh.html). The constant immunoglobulin heavy chain sequences were assembled from the respective fragment sequences of the constant heavy (CH) domains and hinge (H) regions. A single representative allele for each immunoglobulin gene sequence was kept in the working protein database. The contaminants FASTA file from the installation folder of the MaxQuant software was processed to remove all bovine contaminants. Database searches were performed on MaxQuant v 1.5.3.30 against the three databases described above combined, using default settings unless otherwise specified. The built-in contaminants feature of MaxQuant was deactivated. Digestion mode was set to specific against Trypsin/P and GluC, allowing a maximum of two missed cleavages. Methionine oxidation, protein N-terminus acetylation, and serine and threonine phosphorylation were searched as variable modifications. Cysteine carbamidomethylation was set as a fixed modification. Minimum peptide length was allowed at five amino acids, and maximum peptide mass was limited at 10,000 Da. Protein quantification was performed on a minimum of two unique + razor peptides. Label-free quantification was carried out using the intensity based absolute quantification (iBAQ) values. FTMS recalibration was activated. Following the database search, the protein groups table was further post-processed to remove non-bovine contaminants, reverse identifications, variable immunoglobulin sequences, proteins identified by less than two unique peptides, and proteins identified with an Andromeda score below 20. Supplementary Fig. S14 illustrates the shortcomings of commonly-used SwissProt and UniProt bovine protein databases, and the advantages of using our optimized bovine protein database.
Gazi I., Reiding K.R., Groeneveld A., Bastiaans J., Huppertz T, & Heck A.J. (2023). Key changes in bovine milk immunoglobulin G during lactation: NeuAc sialylation is a hallmark of colostrum immunoglobulin G N-glycosylation. Glycobiology, 33(2), 115-125.
Publication 2023
Acetylation Alleles Amino Acids Amino Acid Sequence Bos taurus Cysteine Cytokinesis DA10 Digestion Gene Products, Protein Genes Genes, vif Immunoglobulin A Immunoglobulin Domains Immunoglobulin Heavy Chains Immunoglobulins Methionine nucleoprotein, Measles virus Peptides Phosphorylation Proteins Proteome Serine Threonine TNFSF14 protein, human Trypsin

Top products related to «Immunoglobulin A»

1
Bovine serum albumin (bsa) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Japan, France, Sao Tome and Principe, Canada, Macao, Spain, Switzerland, Australia, India, Israel, Belgium, Poland, Sweden, Denmark, Ireland, Hungary, Netherlands, Czechia, Brazil, Austria, Singapore, Portugal, Panama, Chile, Senegal, Morocco, Slovenia, New Zealand, Finland, Thailand, Uruguay, Argentina, Saudi Arabia, Romania, Greece, Mexico
Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
2
Nunc maxisorp by Thermo Fisher Scientific
Sourced in United States, Denmark, Germany, United Kingdom, Japan, France
The Nunc MaxiSorp is a high-binding 96-well microplate designed for use in ELISA and other protein-based assays. It features a hydrophilic polystyrene surface that is optimized for the adsorption of proteins and other biomolecules.
3
Igg2a by Southern Biotech
Sourced in United States
IgG2a is an immunoglobulin subclass that functions as an antibody. It is produced by plasma B cells and plays a role in the adaptive immune response.
4
Microplate reader by Bio-Rad
Sourced in United States, China, Japan, Italy, Germany, United Kingdom, Switzerland, France, Canada, Netherlands, Australia, Belgium, India
The Microplate reader is a laboratory instrument used to measure the absorbance or fluorescence of samples in a microplate format. It can be used to conduct various assays, such as enzyme-linked immunosorbent assays (ELISA), cell-based assays, and other biochemical analyses. The core function of the Microplate reader is to precisely quantify the optical properties of the samples in a multi-well microplate.
5
O phenylenediamine dihydrochloride by Merck Group
Sourced in United States, United Kingdom, Macao, India, Germany
O-phenylenediamine dihydrochloride is a chemical compound used in various laboratory applications. It is a white to light gray crystalline powder. The compound can be used as a reagent in analytical and diagnostic procedures.
6
Elisa plate by Corning
Sourced in United States
ELISA plates are a type of laboratory equipment used in enzyme-linked immunosorbent assay (ELISA) techniques. They are multi-well plates, typically made of polystyrene, that are designed to facilitate the detection and quantification of various biomolecules, such as proteins, antibodies, or antigens, within a sample.
7
Elisa plate by Thermo Fisher Scientific
Sourced in Denmark, United States, United Kingdom
ELISA (Enzyme-Linked Immunosorbent Assay) plates are a type of laboratory equipment used for performing enzyme-linked immunosorbent assays. These plates typically consist of a flat surface with multiple wells, allowing for the simultaneous analysis of multiple samples or conditions. The wells are designed to facilitate the binding of specific proteins or other molecules to the plate surface, enabling the detection and quantification of target analytes in the samples.
8
Maxisorp elisa plate by Thermo Fisher Scientific
Sourced in Denmark, United States, United Kingdom
MaxiSorp ELISA plates are a type of laboratory equipment used for enzyme-linked immunosorbent assays (ELISA). These plates have a high-binding surface that enables efficient capture and detection of target analytes in ELISA experiments.

More about "Immunoglobulin A"

Immunoglobulin A (IgA) is a crucial class of antibodies that play a vital role in the mucosal immune system.
IgA, also known as secretory immunoglobulin, is the predominant immunoglobulin found in bodily secretions such as saliva, tears, and mucus, where it helps safeguard the body against pathogens and allergens.
It is also present in the blood and other bodily fluids.
IgA can exist in monomeric, dimeric, and secretory forms, each with distinct functionalities.
Research on IgA is essential for understanding the mucosal immune response, as well as its involvement in various diseases and conditions, such as allergies, infections, and autoimmune disorders.
To optimize your IgA research, PubCompare.ai can be a valuable tool.
This AI-driven platform provides access to a wealth of protocols from literature, preprints, and patents, and leverages advanced comparisons to help you identify the best protocols and products for your studies.
This can enhance the reproducibility and accuracy of your IgA research.
When conducting IgA studies, you may also encounter related terms and techniques, such as Bovine serum albumin (BSA), a commonly used protein in immunoassays like ELISA; Nunc MaxiSorp, a specialized ELISA plate with high-binding capacity; IgG2a, another class of antibodies; Microplate readers, used to measure absorbance in ELISA; O-phenylenediamine dihydrochloride, a substrate for colorimetric ELISA; and MaxiSorp ELISA plates, designed for high-binding capacity and optimal results.
Incorporating these terms and techniques can further enhance your understanding and approach to IgA research.