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Anti-SARS-CoV-2 Antibody IgG Titer Serologic Assay Kit (Spike RBD)

For research use only.

组分(Materials Provided)

IDComponentsSize
RAS024-C01Pre-coated SARS-CoV-2 Spike RBD Microplate1 plate
RAS024-C02SARS-CoV-2 Antibody Positive Control100 μL
RAS024-C03SARS-CoV-2 Antibody Negative Control100 μL
RAS024-C04HRP-Anti-Human IgG200 μL
RAS024-C0510xWashing Buffer50 mL
RAS024-C06Dilution Buffer50 mL
RAS024-C07Substrate Solution12 mL
RAS024-C08Stop Solution7 mL

产品概述(Product Overview)

The newly identified Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has posed a serious threat to human health. A rapid and effective Assay kit detecting the levels of anti-SARS-CoV-2 in human serum can facilitate research on characterization of antibodies produced in response to SARS-CoV-2 infection.

应用说明(Application)

This kit is developed for titer measurement of Anti-SARS-CoV-2 Antibody IgG (Spike RBD) in human serum.

It is for research use only.

重构方法(Reconstitution)

Please see Certificate of Analysis for details of reconstitution instruction and specific concentration.

存储(Storage)

1. Unopened kit should be stored at 2℃-8℃ upon receiving.

2. Find the expiration date on the outside packaging and do not use reagents past their expiration date.

3. The opened kit should be stored per components table. The shelf life is 30 days from the date of opening.

原理(Assay Principles)

This assay kit employs a standard indirect-ELISA format, providing a rapid detection of Anti-SARS-CoV-2 antibodies in serum by SARS-CoV-2 Spike RBD. The kit consists of Pre-coated SARS-CoV-2 Spike RBD Microplate, an Positive Control, an Negative Control,an HRP-Anti-Human IgG secondary antibody and related buffer.

Your experiment will include 4 simple steps:

a) Add your sample to the plate, take the Anti-SARS-CoV-2 antibody as Control sample. The samples and Control sample are diluted by Blocking / Dilution Buffer.

b) Add diluted Secondary antibody HRP-Anti-Human IgG to the plate. The Secondary antibody is diluted by Blocking / Dilution Buffer.

c) Wash the plate and add TMB or other colorimetric HRP substrate.

d) Stop the substrate reaction by add diluted acid. Absorbance (OD) is calculate as the absorbance at 450 nm minus the absorbance at 630 nm to remove background prior to statistical analysis. The OD Value reflects the amount of antibody bound.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

典型数据-Typical Data Please refer to DS document for the assay protocol.

Spike RBD TYPICAL DATA

Detection of Monoclonal Anti-SARS-CoV-2 Antibody, Human IgG1 titer by Indirect-ELISA Assay.
Immobilized SARS-CoV-2 Spike RBD at 2 μg/mL (100 μL/well) can bind Monoclonal Anti-SARS-CoV-2 Antibody, Human IgG1 in 1:400 human serum. Detection was performed using HRP-Anti-human IgG antibody with sensitivity of 98 ng/mL (QC tested).

 
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前沿进展

Within-Host Fitness and Antigenicity Shift Are Key Factors Influencing the Prevalence of Within-Host Variations in the SARS-CoV-2 S Gene
Xi, Hua, Jiang et al
Viruses (2025) 17 (3)
Abstract: Within-host evolution plays a critical role in shaping the diversity of SARS-CoV-2. However, understanding the primary factors contributing to the prevalence of intra-host single nucleotide variants (iSNVs) in the viral population remains elusive. Here, we conducted a comprehensive analysis of over 556,000 SARS-CoV-2 sequencing data and prevalence data of different SARS-CoV-2 S protein amino acid mutations to elucidate key factors influencing the prevalence of iSNVs in the SARS-CoV-2 S gene. Within-host diversity analysis revealed the presence of mutational hotspots within the S gene, mainly located in NTD, RBD, TM, and CT domains. Additionally, we generated a single amino acid resolution selection status map of the S protein. We observed a significant variance in within-host fitness among iSNVs in the S protein. The majority of iSNVs exhibited low to no within-host fitness and displayed low alternate allele frequency (AAF), suggesting that they will be eliminated due to the narrow transmission bottleneck of SARS-CoV-2. Notably, iSNVs with moderate AAFs (0.06-0.12) were found to be more prevalent than those with high AAFs. Furthermore, iSNVs with the potential to alter antigenicity were more prevalent. These findings underscore the significance of within-host fitness and antigenicity shift as two key factors influencing the prevalence of iSNVs in the SARS-CoV-2 S gene.
Serological Assays Reveal No Evidence of Natural SARS-CoV-2 Infection in US Cattle
Ramasamy, Quraishi, Mukherjee et al
Microorganisms (2025) 13 (3)
Abstract: Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) continues to pose a significant threat to public health. Notably, SARS-CoV-2 demonstrates the capacity to infect various non-human animal species, including both captive and free-living animals. Earlier experimental studies revealed low susceptibility of domestic cattle (Bos taurus) to ancestral B.1 lineage; however, recent experimental findings indicate greater permissiveness of cattle to SARS-CoV-2 Delta variant. While some studies detected evidence of SARS-CoV-2 infection in cattle in Italy, Germany, India, and Nigeria, currently, there is no evidence of SARS-CoV-2 infections in US cattle. We have investigated over 600 samples, including pre-pandemic and pandemic cattle sera collected from Pennsylvania for the presence of SARS-CoV-2 antibodies. Since serological tests have inherent problems of false positives and negatives, we conducted a comprehensive assessment of multiple serological assays. As there are no known SARS-CoV-2 positive cattle serum samples, we used hyperimmune serum raised in cattle with SARS-CoV-2-spike receptor binding domain (RBD) as positive control for the test validation. We found that pseudovirus neutralization assays with a luciferase reporter system can produce false positive results, and care must be taken to interpret serological diagnosis using these assays. We found no serological evidence of natural SARS-CoV-2 infection or transmission among cattle in the US. This study underscores the importance of robust evaluation when employing serological assays for SARS-CoV-2 detection in cattle populations.
Conformational and Stability Analysis of SARS-CoV-2 Spike Protein Variants by Molecular Simulation
Olivos-Ramirez, Cofas-Vargas, Madl et al
Pathogens (2025) 14 (3)
Abstract: We performed a comprehensive structural analysis of the conformational space of several spike (S) protein variants using molecular dynamics (MD) simulations. Specifically, we examined four well-known variants (Delta, BA.1, XBB.1.5, and JN.1) alongside the wild-type (WT) form of SARS-CoV-2. The conformational states of each variant were characterized by analyzing their distributions within a selected space of collective variables (CVs), such as inter-domain distances between the receptor-binding domain (RBD) and the N-terminal domain (NTD). Our primary focus was to identify conformational states relevant to potential structural transitions and to determine the set of native contacts (NCs) that stabilize these conformations. The results reveal that genetically more distant variants, such as XBB.1.5, BA.1, and JN.1, tend to adopt more compact conformational states compared to the WT. Additionally, these variants exhibit novel NC profiles, characterized by an increased number of specific contacts distributed among ionic, polar, and nonpolar residues. We further analyzed the impact of specific mutations, including T478K, N500Y, and Y504H. These mutations not only enhance interactions with the human host receptor but also alter inter-chain stability by introducing additional NCs compared to the WT. Consequently, these mutations may influence the accessibility of certain protein regions to neutralizing antibodies. Overall, these findings contribute to a deeper understanding of the structural and functional variations among S protein variants.
The Use of Heterologous Antigens for Biopanning Enables the Selection of Broadly Neutralizing Nanobodies Against SARS-CoV-2
Aripov, Zaykovskaya, Mechetina et al
Antibodies (Basel) (2025) 14 (1)
Abstract: Background: Since the emergence of SARS-CoV-2 in the human population, the virus genome has undergone numerous mutations, enabling it to enhance transmissibility and evade acquired immunity. As a result of these mutations, most monoclonal neutralizing antibodies have lost their efficacy, as they are unable to neutralize new variants. Antibodies that neutralize a broad range of SARS-CoV-2 variants are of significant value in combating both current and potential future variants, making the identification and development of such antibodies an ongoing critical goal. This study discusses the strategy of using heterologous antigens in biopanning rounds. Methods: After four rounds of biopanning, nanobody variants were selected from a phage display library. Immunochemical methods were used to evaluate their specificity to the S protein of various SARS-CoV-2 variants, as well as to determine their competitive ability against ACE2. Viral neutralization activity was analyzed. A three-dimensional model of nanobody interaction with RBD was constructed. Results: Four nanobodies were obtained that specifically bind to the receptor-binding domain (RBD) of the SARS-CoV-2 spike glycoprotein and exhibit neutralizing activity against various SARS-CoV-2 strains. Conclusions: The study demonstrates that performing several rounds of biopanning with heterologous antigens allows the selection of nanobodies with a broad reactivity spectrum. However, the fourth round of biopanning does not lead to the identification of nanobodies with improved characteristics.
Showing 1-4 of 5098 papers.
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