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Immunoglobulin G

Immunoglobulin G (IgG) is a class of antibodies that play a crucial role in the adaptive immune response.
IgG molecules are large, Y-shaped glycoproteins composed of two heavy and two light chains.
They are the most abundant type of antibody found in the blood and extracellular fluid, accounting for approximately 75% of all serum antibodies in humans.
IgG antibodies are responsible for a wide range of functions, including neutralization of toxins and viruses, opsonization of pathogens for phagocytosis, and activation of the complement system.
They are also involved in the regulation of the immune response and the clearance of immune complexes.
Understanding the structure, function, and regulation of IgG is essential for the study of immune system dynamics and the development of therapies targeting humoral immunity.
PubCompare.ai leverages AI to enhance IgG research by comparing protocols from literature, preprints, and patents, helping researchers optimize their studies with the most reproducible and accurate methods.

Most cited protocols related to «Immunoglobulin G»

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
FRET Biosensor Assay in HeLa and Cos7 Cells
Cited 35 times
HeLa cells were purchased from the Human Science Research Resources Bank (Sennanshi, Japan). The Cos7 cells used were Cos7/E3, a subclone of Cos7 cells established by Y. Fukui (National Research Institute of Health, Taiwan, Republic of China). HeLa cells and Cos7 cells were maintained in DMEM (Sigma-Aldrich, St. Louis, MO) supplemented with 10% FBS. The cells were plated on 35-mm glass base dishes or 96-well glass base plates (Asahi Techno Glass, Tokyo, Japan), which were coated with collagen type I (Nitta Gelatin, Osaka, Japan). Plasmids encoding FRET biosensors were transfected into HeLa cells and Cos7 cells by 293fectin or Lipofectamine 2000, according to the manufacturer's instructions (Invitrogen, San Diego, CA), respectively. EGF was purchased from Sigma-Aldrich. dbcAMP, TPA, Calyculin A, Anisomycin, PD153035, and JNK inhibitor VIII were purchased from Calbiochem (La Jolla, CA). PD184352 was obtained from Toronto Research Chemicals (Ontario, Canada). BI-D1870 was purchased from Symansis (Shanghai, China). Rapamycin was obtained from LC Laboratories (Woburn, MA). PLX-4720 was purchased from Selleck Chemicals (Houston, TX). The expression vector of piggyBac transposase was provided by A. Bradley (Wellcome Trust Sanger Institute, Cambridge, UK; Yusa et al., 2009 (link)). Phos-tag was obtained from the Phos-tag Consortium (Hiroshima, Japan; www.phos-tag.com). Anti-green fluorescence protein (GFP) sera were prepared in our laboratory. LI-COR (Lincoln, NE) blocking buffer and the IRDye680- and IRDye800-conjugated anti–rabbit and anti–mouse immunoglobulin G secondary antibodies were obtained from LI-COR.
Komatsu N., Aoki K., Yamada M., Yukinaga H., Fujita Y., Kamioka Y, & Matsuda M. (2011). Development of an optimized backbone of FRET biosensors for kinases and GTPases. Molecular Biology of the Cell, 22(23), 4647-4656.
Publication 2011
1,3-bis(bis(pyridin-2-ylmethyl)amino)propan-2-ol Anisomycin Anti-Antibodies BI D1870 Biosensors Bucladesine Buffers calyculin A Cells Cloning Vectors Collagen Type I Fluorescence Resonance Energy Transfer Gelatins Green Fluorescent Proteins HeLa Cells Hyperostosis, Diffuse Idiopathic Skeletal Immunoglobulin G IRDye800 lipofectamine 2000 Manpower Mus PD 153035 PD 184352 Plasmids PLX 4720 Rabbits Serum Sirolimus Transposase
3
Expression and Characterization of HHD Monochain
Cited 35 times
Expression of the HHD monochain and lack of H-2Db and H-2Kb were documented by indirect immunofluorescence analyses using B9.12.1 (anti–HLA class I), B22.249.R.19 (anti–H-2Db), and 20.8.4S unlabeled mAb, detected with F(ab)′2 FITC-conjugated goat anti–mouse IgG. Percentages of single CD4+ and CD8+ T lymphocytes were determined by double staining using phycoerythrin-labeled anti–mouse CD4 (CALTAG Labs., South San Francisco, CA) and biotinylated anti–mouse CD8 (CALTAG Labs.) detected with streptavidin– Perc-P (CALTAG Labs.). Expression of the different Vβ TCR were similarly analyzed using phycoerythrin-labeled anti-CD8 mAb (PharMingen, San Diego, CA) and purified, FITC-labeled Vβ2 (B.20.6), Vβ3 (KJ.25), Vβ4 (KT.10.4), Vβ5.1,.2 (MR.9.4), Vβ6 (44.22), Vβ7 (TR 130), Vβ8.1,.2,.3 (F.23.1), Vβ9 (MR. 10.2), Vβ10 (B.21.5), Vβ11 (RR.3.15), Vβ13 (MR.12.4), and Vβ17 (KJ.23.1)- specific mAb. Splenocytes from three individual Db−/−, β2m−/−, HHD+, or HHD− mice were red blood cell depleted and enriched in T lymphocytes by wheat germ agglutinin (Sigma Chemical Co., St Louis, MO) precipitation of B lymphocytes and NK cells as described (18 (link)). Staining of 106 cells was performed in 100 μl of PBS with 0.02% sodium azide for 30 min on ice. Purified mAb or F(ab)′2 were used at 10 μg/ml and F(ab)′2 FITCconjugated goat anti–mouse IgG was used 1:100 diluted. A total of 25,000 1% paraformaldehyde-fixed cells per sample was subjected to one- or two-color analysis on FACScan®.
Pascolo S., Bervas N., Ure J.M., Smith A.G., Lemonnier F.A, & Pérarnau B. (1997). HLA-A2.1–restricted Education and Cytolytic Activity of CD8+ T Lymphocytes from β2 Microglobulin (β2m) HLA-A2.1 Monochain Transgenic H-2Db β2m Double Knockout Mice. The Journal of Experimental Medicine, 185(12), 2043-2051.
Publication 1997
anti-IgG B-Lymphocytes CD8-Positive T-Lymphocytes Cells Erythrocytes Fluorescein-5-isothiocyanate Goat Immunoglobulin G Indirect Immunofluorescence Mus Natural Killer Cells paraform Phycoerythrin Sodium Azide Streptavidin T-Lymphocyte Wheat Germ Agglutinins
4
Pneumococcal Vaccine Response in HIV-Exposed Infants
Cited 28 times
The study enrolled a priori four groups of children aged 6 to 12 weeks. These included 2 groups of HIV infected infants, co-enrolled from the Children with HIV Early Antiretroviral (CHER) Study in South Africa, 5 (link) with CD4+ T-lymphocyte cells ≥25% randomized to initiate ART immediately (HIV+/ART+ group); or ART was initiated when clinically or immunologically indicated (HIV+/ART− Group). 6 The ART regimen included zidovudine, lamivudine and lopinavir/ritonavir. Additionally, two cohorts of HIV non-infected infants were prospectively enrolled in parallel to the HIV infected children including: i. infants born to HIV infected mothers who were HIV PCR (Roche Amplicor Version 1.5 RNA PCR) negative at baseline and one month after the third dose of Vaccine (M+/I−) and ii. infants born to mothers seronegative for HIV after 24 weeks of gestational age during pregnancy and who were HIV ELISA seronegative at study-enrolment (i.e. M−/I−).
Additional participant-eligibility criteria included absence of intercurrent illness within 72 hours of enrolment, no Grade 3 or 4 clinical or laboratory toxicity as per DAIDS Pediatric Adverse Experiences,7 birth weight of at least 2000 grams, participation in the CHER study for HIV infected infants, absence of receipt of any blood products prior to study entry, any immunomodulating medication for more than two weeks within one week of possible enrolment
Infants were enrolled between April 2005 and June 2006 and scheduled to receive three doses of 7-valent pneumococcal conjugate vaccine (i.e. Prevnar®; Wyeth Vaccines, NJ, USA) at 6 to 12, 9 to 18 and 12 to 24 weeks of age. Infants received other scheduled childhood vaccines, included in the public immunization program, concurrently with Prenar®.
Immune response to the primary series of Vaccine was measured 3 to 6 weeks after the third dose using serum from venous blood which had been centrifuged, aliquotted and stored at –20 to −70°C until processing at the Respiratory and Meningeal Pathogens Research Unit (RMPRU), Johannesburg, South Africa. A standardized enzyme immunoassay (EIA), including adsorption with 22F polysaccharide, was used to test for vaccine-serotype specific capsular IgG antibody concentrations as described. 8 (link) 9 (link)
The functionality of the antibodies post vaccination was determined by opsonophagocytic killing assay (OPA) for serotypes 9V, 19F and 23F using differentiated HL-60 cells as described.8 (link) 10 (link) Lower antibody concentrations required for 50% killing activity on OPA is suggestive of superior antibody functional activity. Detectable killing activity on OPA was defined as a titer of ≥8.
For quality assurance, a quality control serum from a vaccinated volunteer was included on each plate. The coefficient of variation for the control sera were <40% for all serotypes.
Madhi S.A., Adrian P., Cotton M.F., McIntyre J.A., Jean-Philippe P., Meadows S., Nachman S., Käyhty H., Klugman K.P, & Violari A. (2010). Effect of HIV infection status and anti-retroviral treatment on quantitative and qualitative antibody responses to pneumococcal conjugate vaccine in infants. The Journal of infectious diseases, 202(3), 355-361.
Publication 2010
Adsorption Antibodies Biological Assay Birth Weight Blood Capsule CD4 Positive T Lymphocytes Cells Child Childbirth Eligibility Determination Enzyme-Linked Immunosorbent Assay Enzyme Immunoassay Gestational Age HIV-2 HL-60 Cells Immunization Programs Immunoglobulin G Infant Lamivudine lopinavir-ritonavir drug combination Meninges Mothers pathogenesis Pharmaceutical Preparations Pneumococcal Vaccine Polysaccharides Pregnancy Prevnar Respiratory Rate Response, Immune Serum Treatment Protocols Vaccination Vaccines Veins Voluntary Workers Zidovudine
5
Comprehensive Repeat Annotation of CHM13
Cited 26 times
A very brief methods overview is provided here. Detailed methods are provided in (42 ). Repeats in the T2T-CHM13 assembly were annotated by parsing and combining output from RepeatMasker [provided in (40 (link))] along with custom-built pipelines for annotating αSat and HSat2,3 (42 ). Regions identified as “SAR” by RepeatMasker were annotated as HSat1A, and regions annotated as “HSATI” by RepeatMasker were annotated as HSat1B. αSat HOR-haps were identified by (i) generating multiple alignments of all HOR units (or subregions of HOR units) from an array, (ii) deriving a consensus sequence, (iii) recoding the individual sequences into binary vectors based on matches to the consensus, and (iv) clustering these binary vectors by use of k-means clustering. Phylogenetic analyses of αSat sequences were performed with MEGA5. Dotplots colored by percent identity were produced with StainedGlass (88 (link)).
To analyze short-read NChIP-seq and CUT&RUN data, two parallel methods were developed: (i) marker-assisted mapping to the T2T-CHM13 reference and (ii) reference-free region-specific marker enrichment. For marker-assisted mapping, reads were aligned to the reference then filtered to include only alignments that overlap precomputed nucleotide oligomers of length k (k-mers) that occur in only one distinct position in the reference. For reference-free enrichment analysis, a set of k-mers that are enriched in CENP-A–targeted sequencing reads (relative to reads from input or immunoglobulin G controls) were first identified. Next, these enriched k-mers were compared with precomputed k-mers in the reference that occur exclusively within a single window of a given size (“region-specific markers”). Windows with multiple matches to enriched k-mers were reported as enriched for CENP-A. We performed a similar analysis using HOR-hap–specific markers on chrX, to reveal the broad enrichment of CENP-A on each HOR-hap across multiple individuals (fig. S21).
Altemose N., Glennis A., Bzikadze A.V., Sidhwani P., Langley S.A., Caldas G.V., Hoyt S.J., Uralsky L., Ryabov F.D., Shew C.J., Sauria M.E., Borchers M., Gershman A., Mikheenko A., Shepelev V.A., Dvorkina T., Kunyavskaya O., Vollger M.R., Rhie A., McCartney A.M., Asri M., Lorig-Roach R., Shafin K., Aganezov S., Olson D., de Lima L.G., Potapova T., Hartley G.A., Haukness M., Kerpedjiev P., Gusev F., Tigyi K., Brooks S., Young A., Nurk S., Koren S., Salama S.R., Paten B., Rogaev E.I., Streets A., Karpen G.H., Dernburg A.F., Sullivan B.A., Straight A.F., Wheeler T.J., Gerton J.L., Eichler E.E., Phillippy A.M., Timp W., Dennis M.Y., O'Neill R.J., Zook J.M., Schatz M.C., Pevzner P.A., Diekhans M., Langley C.H., Alexandrov I.A, & Miga K.H. (2022). Complete genomic and epigenetic maps of human centromeres. Science (New York, N.Y.), 376(6588), eabl4178.
Publication 2022
Cloning Vectors Consensus Sequence GPER protein, human Immunoglobulin G Nucleotides

Most recents protocols related to «Immunoglobulin G»

1
Binding Assay of Chimeric Anti-FOLR1 mAbs
Not available on PMC !

Example 6

To assess the binding of the chimeric anti-FOLR1 mAbs to cells that are known to express FOLR1, SK-OV-3 (ATCC® HTB-77™) cells were plated at 80,000 cells per well on a 96-well non-binding U-bottom plate (Greiner Bio-One, Cat #: 650901). In some experiments, 90,000 cells per well were used. The cells were incubated in 50 μL FACS buffer (HBSS with 0.1% BSA and 0.05% sodium azide) containing mAbs at different concentrations on ice for 15 minutes. After wash, cells were incubated in 50 μL FACS buffer containing 3.5 μg/mL F(ab′)2-Goat anti-Human IgG Fc conjugated to Alexa Fluor® 488 (Invitrogen, Cat #: H10120) on ice for 15 minutes in dark and washed again. Cells were analyzed using an Attune NxT flow cytometer. The results for the binding of the chimeric anti-FOLR1 mAbs to SK-OV-3 cells are shown in FIGS. 3A-3D. MFI, mean fluorescence intensity.

US11873335B2. Anti-folate receptor 1 antibodies and uses thereof (2024-01-16). Phanes Therapeutics, Inc. [US]. Inventors: Minghan Wang [US], Hui Zou [US], Haiqun Jia [US].
Full text: Click here
Patent 2024
alexa fluor 488 Buffers Cells Chimera Figs Fluorescence FOLR1 protein, human Goat Hemoglobin, Sickle Homo sapiens Immunoglobulin G Monoclonal Antibodies Sodium Azide
2
Binding Assay for CD25-Expressing Cells
Not available on PMC !

Example 3

Binding to CD25 expressing Karpas 299 cells was examined by staining Karpas299 cells with test articles (anti-CD25 primary antibodies) starting at a concentration of 20 g/ml antibodies followed by semi-log dilution series (7-point) for 30 minutes on ice. This was followed by staining with a secondary antibody (Alexa Fluor 647-AffiniPure F(ab′)2 Fragment Rabbit Anti-Human IgG Fcγ fragment—(Jackson ImmunoResearch)) at a concentration of 1 μg/ml for 30 minutes on ice. All samples were stained in duplicates. Live cells were gated using FSC vs SSC parameters by flow cytometry during sample acquisition. Mean fluorescence intensity (MFI) of stained cells were plotted on an XY chart, graphing MFI against the log of the concentration, and the data fit to a non-linear regression curve from which the EC50 is calculated. Results are shown in FIG. 3.

US11873341B2. Anti-CD25 for tumour specific cell depletion (2024-01-16). Tusk Therapeutics Ltd. [GB], Cancer Research Technology Limited [GB]. Inventors: Anne Goubier [GB], Beatriz Goyenechea Corzo [GB], Josephine Salimu [GB], Kevin Moulder [GB], Pascal Merchiers [GB], Sergio Quezada [GB].
Full text: Click here
Patent 2024
Alexa Fluor 647 Anti-Antibodies anti-IgG Cells Flow Cytometry Fluorescence Homo sapiens IL2RA protein, human Immunoglobulin G Immunoglobulins Rabbits Technique, Dilution
3
Antibody Variants and Cell Killing Assays
Not available on PMC !

Example 10

Several 4D5 liability fixed affinity variants were selected for further characterization. Y55E.H91A.N54E.D98T and Y55E.H91A.N54E.D98T.Y102V variants were formatted into a 1Fab-IgG TDB antibody having a natural (short) linker (hinge; DKTHT, SEQ ID NO: 50) and compared to H91A-1Fab-IgG TDB in a dose response assay to quantify killing of SKBR3 (FIG. 33A) or MCF7 (FIG. 33B) target cells. Each well was seeded with 1.5×104 SKBR3 or MCF7 target cells and co-cultured with PMBC-derived CD8+ effector cells at a 1:3 effector:target ratio. Results are summarized in Table 12, below.

TABLE 12
SKBR3 target cell killing by selected 4D5 1Fab-IgG TDB variants
SKBR3MCF7
4D5 1Fab-IgG TDBIC50 (ng/mL)IC50 (ng/mL)
Y55E.H91A.N54E.D98T.Y102V2.61>1,000
Y55E.H91A.N54E.D98T1.63>1,000
Y55E.H91A.N54E.D98T.Y102V1.83>1,000
H91A2.01>1,000

The binding of 4D5 Y55E.H91A.N54E.D98T-1Fab-IgG TDB and 4D5 Y55E.H91A.N54E.D98T.Y102V antibodies to SKBR3 cells (FIG. 34A) and MCF7 cells (FIG. 34B) was also characterized by flow cytometry. In general, 4D5 Y55E.H91A.N54E.D98T.Y102V-1Fab-IgG TDB were similar to 4D5 H91A-1Fab-IgG TDB in terms of cytotoxicity and binding to SKBR3 cells and MCF7 cells.

US11866498B2. Bispecific antigen-binding molecules and methods of use (2024-01-09). Genentech, Inc. [US]. Inventors: Diego Ellerman [US], Teemu T. Junttila [US], Twyla Noelle Lombana [US], Dionysos Slaga [US], Christoph Spiess [US].
Full text: Click here
Patent 2024
Antibodies Biological Assay Cells Cultured Cells Cytotoxin Flow Cytometry Immunoglobulin G MCF-7 Cells
4
FACS Screening of GPRC5D Phage Clones
Not available on PMC !

Example 4

FACS Screening: FIG. 24 shows FACS analysis of GPRC5D-specific phage antibody clones (ET150-1, ET150-2, ET150-5, ET150-8, ET150-18). Phage clones were incubated with 3T3-GPRC5D cell line, then with anti-M13 mouse antibody. Finally APC-labeled anti-mouse IgG 2nd antibody was added to the reaction after washing again. The binding was measured by FACS and expressed as mean fluorescence intensity (MFI). Cells incubated with M13 K07 helper phage and cells only were used as negative controls.

US11866478B2. Nucleic acid molecules encoding chimeric antigen receptors targeting G-protein coupled receptor (2024-01-09). MEMORIAL SLOAN KETTERING CANCER CENTER [US], EUREKA THERAPEUTICS, INC. [US]. Inventors: Renier J. Brentjens [US], Eric L Smith [US], Cheng Liu [US].
Full text: Click here
Patent 2024
3T3 Cells Anti-Antibodies Antibodies, Anti-Idiotypic Bacteriophage M13 Bacteriophages Cell Lines Cells Clone Cells Fluorescence GPRC5D protein, human Immunoglobulin G Immunoglobulins Mus
5
Evaluation of Targeted Nanoparticle Tumor Accumulation
Not available on PMC !

Example 2

Mice were injected via subcutaneous injection with lymphoma cells and tumors allowed to form. Mice received intravenous (IV) injection of equal amounts of alexaflor 750-labeled ABRAXANE (ABX), ABRAXANE coated with non-specific antibodies (AB IgG), or AR160.

Twenty-four hours after IV injection, tumor accumulation of the respective treatments was determined based on a fluorescence threshold. Background was determined based on a region of the mouse without a tumor. FIG. 1 is a graphical representation of background and tumor fluorescence. Table 8 indicates the numerical values for each, including tumor-associated fluorescence (average radiant efficiency from the tumor minus background). Addition of rituximab to the ABRAXANE nanoparticle (AR160) results in a nearly 100% increase in tumor uptake of ABRAXANE.

TABLE 8
Average Radiant Efficiency and Adjusted Tumor-Associated Fluorescence
Tumor-
associated
BackgroundTumorFluorescence
ABX1.5412.090.549
AB IgG1.40051.990.5895
AR1601.5452.6371.092

US11878061B2. Methods for improving the therapeutic index for a chemotherapeutic drug (2024-01-23). Mayo Foundation for Medical Education and Research [US]. Inventors: Svetomir N. Markovic [US], Wendy K. Nevala [US].
Full text: Click here
Patent 2024
Abraxane Antibodies Cells Fluorescence Immunoglobulin G Lymphoma Mus Neoplasms Rituximab Subcutaneous Injections

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More about "Immunoglobulin G"

Immunoglobulin G (IgG) is a critical class of antibodies that play a vital role in the adaptive immune response.
These large, Y-shaped glycoproteins are composed of two heavy and two light chains, and are the most abundant type of antibody found in the blood and extracellular fluid, accounting for approximately 75% of all serum antibodies in humans.
IgG antibodies are responsible for a wide range of functions, including neutralization of toxins and viruses, opsonization of pathogens for phagocytosis, and activation of the complement system.
They are also involved in the regulation of the immune response and the clearance of immune complexes.
Understanding the structure, function, and regulation of IgG is essential for the study of immune system dynamics and the development of therapies targeting humoral immunity.
PubCompare.ai leverages AI to enhance IgG research by comparing protocols from literature, preprints, and patents, helping researchers optimize their studies with the most reproducible and accurate methods.
This includes utilizing tools like the Magna RIP RNA-Binding Protein Immunoprecipitation Kit, PVDF membranes, Bovine serum albumin, DAPI, FBS, Protease inhibitor cocktail, EZ-Magna RIP kit, and RIPA lysis buffer to ensure the most robust and reliable results.
By incorporating synonyms, related terms, abbreviations, and key subtopics, researchers can gain a comprehensive understanding of Immunoglobulin G and its critical role in the immune system.
This AI-powered approach to protocol comparison and optimization can help drive breakthroughs in IgG research and the development of innovative therapies targeting humoral immunity.