Mouse IgG2a ELISA Kit

Name: Mouse IgG2a ELISA Kit
SKU: DEIA655
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

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COA

SDS

Datasheet

Sample

Serum, Plasma

Species Reactivity

Mouse

Detection Method

Sandwich-ELISA

Intended Use

This enzyme linked immunosorbent assay (ELISA) is for the detection of Mouse IgG2a in serum or plasma. Due to idiotypic and allotypic variations, this product may not accurately quantitate hybridomas, monoclonals or myelomas.

Contents of Kit

No.	Components	Size	Storage Conditions
1	Mouse IgG2a Pre-Coated 96-well Strip Plate	1 each	2-8°C
2	Mouse IgG2a Standard, 500 ng/vial	2 each	2-8°C
3	Mouse IgG2a Detection Antibody	12 ml	2-8°C
4	10× Dilution Buffer B	25 ml	2-8°C
5	HRP Solution A	12 ml	2-8°C
6	TMB Substrate	12 ml	2-8°C
7	Stop Solution	12 ml	2-8°C
8	20× Wash Buffer	50 ml	2-8°C
9	Sealing Tape	6 sheets

Storage

Stored at 2-8°C for 6 months from date of receipt.

General Description

There are five classes of mammalian immunoglobulins: IgA, IgD, IgE, IgM, and IgG. In mice, the IgG class is the most abundant (Junqueira, Luiz C. & Jose Carneiro, 2003) and can be further divided into four subclasses: IgG1, IgG2a/IgG2c (strain specific), IgG2b, and IgG3. The general immunoglobulin structure is composed of four polypeptide chains, two heavy and two light chains linked together and to each other by disulfide bonds, creating a tetrameric quaternary structure. The resulting tetramer creates two identical halves which together form a Y like structure. IgG2a has a serum half-life of 5 days and a mean serum concentration of approximately 4.2 mg/ml. Mouse IgG2a can cross the placenta by means of FcRn transcytosis, is cytolytic for macrophages, and causes a heterologous PCA reaction. IgG2a is preferentially expressed in the host in the presence of a viral infection (Quimby & Luong Richard, 2007).

Standard Curve

This typical standard curve was generated using the Mouse IgG2a ELISA Kit Protocol. This standard curve is for demonstration only. A standard curve must be generated for each assay.

*Suggested standard curve points are 500 ng/ml, 167 ng/ml, 55.6 ng/ml, 18.5 ng/ml, 6.17 ng/ml, 2.06 ng/ml, 0.69 ng/ml, and 0 ng/ml. Assay Range: 0.69 – 500 ng/ml

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Datasheet

Certificate of Analysis

Safety Data Sheet

Immunoassays for Process-related Impurities

Customer Reviews

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The antibody response to the glycan alpha-Gal correlates with COVID-19 disease symptoms

JOURNAL OF MEDICAL VIROLOGY

Authors: Miguel Urra, Jose; Ferreras-Colino, Elisa; Contreras, Marinela; Cabrera, Carmen M.; Fernandez de Mera, Isabel G.; Villar, Margarita; Cabezas-Cruz, Alejandro; Gortazar, Christian; de la Fuente, Jose

Abstract

The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has affected millions of people worldwide. Characterization of the immunological mechanisms involved in disease symptomatology and protective response is important to progress in disease control and prevention. Humans evolved by losing the capacity to synthesize the glycan Gal alpha 1-3Gal beta 1-(3)4GlcNAc-R (alpha-Gal), which resulted in the development of a protective response against pathogenic viruses and other microorganisms containing this modification on membrane proteins mediated by anti-alpha-Gal immunoglobulin M (IgM)/IgG antibodies produced in response to bacterial microbiota. In addition to anti-alpha-Gal antibody-mediated pathogen opsonization, this glycan induces various immune mechanisms that have shown protection in animal models against infectious diseases without inflammatory responses. In this study, we hypothesized that the immune response to alpha-Gal may contribute to the control of COVID-19. To address this hypothesis, we characterized the antibody response to alpha-Gal in patients at different stages of COVID-19 and in comparison with healthy control individuals. The results showed that while the inflammatory response and the anti-SARS-CoV-2 (Spike) IgG antibody titers increased, reduction in anti-alpha-Gal IgE, IgM, and IgG antibody titers and alteration of anti-alpha-Gal antibody isotype composition correlated with COVID-19 severity. The results suggested that the inhibition of the alpha-Gal-induced immune response may translate into more aggressive viremia and severe disease inflammatory symptoms. These results support the proposal of developing interventions such as probiotics based on commensal bacteria with alpha-Gal epitopes to modify the microbiota and increase alpha-Gal-induced protective immune response and reduce severity of COVID-19.

Efficient Plant Production of Recombinant NS1 Protein for Diagnosis of Dengue

FRONTIERS IN PLANT SCIENCE

Authors: Xisto, Mariana Fonseca; Dias, Roberto Sousa; Feitosa-Araujo, Elias; Prates, John Willians Oliveira; da Silva, Cynthia Canedo; de Paula, Sergio Oliveira

Abstract

Dengue fever is endemic in more than 120 countries, which account for 3.9 billion people at risk of infection worldwide. The absence of a vaccine with effective protection against the four serotypes of this virus makes differential molecular diagnosis the key step for the correct treatment of the disease. Rapid and efficient diagnosis prevents progression to a more severe stage of this disease. Currently, the limiting factor in the manufacture of dengue (DENV) diagnostic kits is the lack of large-scale production of the non-structural 1 (NS1) protein (antigen) to be used in the capture of antibodies from the blood serum of infected patients. In this work, we use plant biotechnology and genetic engineering as tools for the study of protein production for research and commercial purposes. Gene transfer, integration and expression in plants is a valid strategy for obtaining large-scale and low-cost heterologous protein production. The authors produced NS1 protein of the dengue virus serotype 2 (NS1DENV2) in the Arabidopsis thaliana plant. Transgenic plants obtained by genetic transformation expressed the recombinant protein that was purified and characterized for diagnostic use. The yield was 203 mu g of the recombinant protein per gram of fresh leaf. By in situ immunolocalization, transgenic protein was observed within the plant tissue, located in aggregates bodies. These antigens showed high sensitivity and specificity to both IgM (84.29% and 91.43%, respectively) and IgG (83.08% and 87.69%, respectively). The study goes a step further to validate the use of plants as a strategy for obtaining large-scale and efficient protein production to be used in dengue virus diagnostic tests.