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 >  Protein>Spike RBD >SPD-C522e

SARS-CoV-2 Spike RBD Protein, His Tag (B.1.1.529/Omicron) (MALS verified)

分子别名(Synonym)

Spike,S protein RBD,Spike glycoprotein Receptor-binding domain,S glycoprotein RBD,Spike protein RBD

表达区间及表达系统(Source)

SARS-CoV-2 Spike RBD, His Tag (B.1.1.529/Omicron) (SPD-C522e) is expressed from human 293 cells (HEK293). It contains AA Arg 319 - Lys 537 (Accession # QHD43416.1 (G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R, N501Y, Y505H)). The spike mutations are identified on the SARS-CoV-2 Omicron variant (Pango lineage: B.1.1.529; GISAID clade: GR/484A; Nextstrain clade: 21K).

Predicted N-terminus: Arg 319

Request for sequence

蛋白结构(Molecular Characterization)

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 26.8 kDa. The protein migrates as 33-38 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>95% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 12 months under sterile conditions after reconstitution.

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
 

电泳(SDS-PAGE)

Spike RBD SDS-PAGE

SARS-CoV-2 Spike RBD, His Tag (B.1.1.529/Omicron) on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

SEC-MALS

Spike RBD SEC-MALS

The purity of SARS-CoV-2 Spike RBD, His Tag (B.1.1.529/Omicron) (Cat. No. SPD-C522e) is more than 90% and the molecular weight of this protein is around 33-48 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

Spike RBD ELISA

Immobilized Human ACE2, Fc Tag (Cat. No. AC2-H5257) at 5 μg/mL (100 μL/well) can bind SARS-CoV-2 Spike RBD, His Tag (B.1.1.529/Omicron) (Cat. No. SPD-C522e) with a linear range of 10-156 ng/mL (QC tested).

Protocol

Spike RBD ELISA

Immobilized SARS-CoV-2 Spike RBD, His Tag (B.1.1.529/Omicron) (Cat. No. SPD-C522e) at 1 μg/mL (100 μL/well) can bind Anti-SARS-CoV-2 Spike RBD Antibody, Chimeric mAb, Human IgG1 (AM130) (Cat. No. S1N-M13A1) with a linear range of 0.1-3 ng/mL (Routinely tested).

Protocol

Spike RBD ELISA

Immobilized SARS-CoV-2 Spike RBD, His Tag (B.1.1.529/Omicron) (Cat. No. SPD-C522e) at 1 μg/mL (100 μL/well) can bind Human ACE2, Fc Tag (Cat. No. AC2-H5257) with a linear range of 0.4-13 ng/mL (Routinely tested).

Protocol

 

活性(Bioactivity)-SPR

Spike RBD SPR

Human ACE2, Fc Tag (Cat. No. AC2-H5257) captured on CM5 chip via human IgG Fc antibody can bind SARS-CoV-2 Spike RBD, His Tag (B.1.1.529/Omicron) (MALS verified) (Cat. No. SPD-C522e) with an affinity constant of 4.56 nM as determined in a SPR assay (Biacore 8K).

Protocol

 

活性(Bioactivity)-BLI

Spike RBD BLI

Loaded Human ACE2, Fc Tag (Cat. No. AC2-H5257) on Protein A Biosensor, can bind SARS-CoV-2 Spike RBD, His Tag (B.1.1.529/Omicron) (MALS verified) (Cat. No. SPD-C522e) with an affinity constant of 11.4 nM as determined in BLI assay (ForteBio Octet Red96e).

Protocol

 
评论(6)
  1. 178XXXXXXX2
  2. 0人赞
  3. 该产品进行实验时,结果稳定且可靠,完全满足我们的实验需求,厂家服务态度好,物流较快,检测效果稳定,使用方便,以后还会继续购买。
  4. 2022-10-9
  1. 188XXXXXXX1
  2. 0人赞
  3. 物流较快,技术服务很好,使用该产品进行实验时,结果稳定且可靠,完全满足我们的实验需求,强烈推荐大家使用该产品哦!
  4. 2022-3-10
  1. 198XXXXXXX5
  2. 0人赞
  3. 同时购买了SPD-C522e货号的蛋白,一直在使用,效果都很好,结果也很稳定,项目顺利交付。还会继续购买acro家的商品。
  4. 2024-2-18
 
ACRO质量管理体系
 
 

背景(Background)

It's been reported that Coronavirus can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

文献引用(Citations)

 

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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