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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

 
 
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

Preemptive optimization of a clinical antibody for broad neutralization of SARS-CoV-2 variants and robustness against viral escape
Zhu, Rajan, Hayes et al
Sci Adv (2025) 11 (13), eadu0718
Abstract: Most previously authorized clinical antibodies against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have lost neutralizing activity to recent variants due to rapid viral evolution. To mitigate such escape, we preemptively enhance AZD3152, an antibody authorized for prophylaxis in immunocompromised individuals. Using deep mutational scanning (DMS) on the SARS-CoV-2 antigen, we identify AZD3152 vulnerabilities at antigen positions F456 and D420. Through two iterations of computational antibody design that integrates structure-based modeling, machine-learning, and experimental validation, we co-optimize AZD3152 against 24 contemporary and previous SARS-CoV-2 variants, as well as 20 potential future escape variants. Our top candidate, 3152-1142, restores full potency (100-fold improvement) against the more recently emerged XBB.1.5+F456L variant that escaped AZD3152, maintains potency against previous variants of concern, and shows no additional vulnerability as assessed by DMS. This preemptive mitigation demonstrates a generalizable approach for optimizing existing antibodies against potential future viral escape.
Role of N-linked glycosylation sites in human ACE2 in SARS-CoV-2 and hCoV-NL63 infection
Noettger, Zech, Nchioua et al
J Virol (2025)
Abstract: Angiotensin-converting enzyme 2 (ACE2) is a transmembrane protein known for its physiological role in the renin-angiotensin system that also serves as a receptor for entry of SARS-CoV-1, SARS-CoV-2, and the seasonal human coronavirus NL63 (hCoV-NL63). ACE2 contains seven N-linked glycosylation sites. Molecular simulation and binding analyses suggest that some of them are involved in the interaction with the Spike (S) proteins of hCoVs, but their relevance in S-mediated fusion and viral entry is poorly investigated. To address this, we determined the impact of all seven N-linked glycosylation sites in ACE2 on S-mediated SARS-CoV-2 and hCoV-NL63 infection as well as cell-to-cell fusion. We found that all mutant ACE2 proteins are expressed and localized at the cell surface, albeit ACE2 lacks all glycans at decreased levels. On average, changes in T92I, N322A, and N690A, as well as combined mutation of all N-linked glycosylation sites increased endocytic VSVpp infection mediated by early HU-1 as well as Omicron BA.2, BA.5, and XBB.1.5 SARS-CoV-2 S proteins. In comparison, only the lack of glycan at N322 in ACE2 enhanced syncytia formation and only in the case of HU-1 and XBB.1.5 S proteins. Changes in N90A, T92I, and N322A increased infection by the early SARS-CoV-2 HU-1 strain about twofold to threefold but had lesser effects on infection by genuine Omicron variants. Despite reduced cell surface expression of ACE2, elimination of all N-linked glycosylation sites usually enhanced SARS-CoV-2 infection via the endocytic pathway while having little effect on entry at the cell surface in the presence of TMPRSS2. Our results provide insights into the role of N-linked glycans in the ability of human ACE2 (hACE2) to serve as receptors for coronavirus infection.Several human coronaviruses use angiotensin-converting enzyme 2 (ACE2) as a primary receptor for infection of human cells. ACE2 is glycosylated at seven distinct positions, and the role of glycans for the entry of SARS-CoV-2 and hCoV-NL63 into their target cells is incompletely understood. Here, we examined the impact of individual and combined mutations in hACE2 glycosylation sites on Spike-mediated VSV-pseudoparticle and genuine SARS-CoV-2 and hCoV-NL63 infection and cell-to-cell fusion. Our results provide new information on the role of glycans in hACE2 for infection by highly pathogenic and seasonal coronaviruses.
Patient-specific mutation of a contact site protein Tomm70 causes neurodegeneration in a zebrafish model
Garg, Heinrich, Perera et al
Dis Model Mech (2025)
Abstract: Tomm70 is a receptor at the contact site between mitochondria and the endoplasmic reticulum, and has been identified as a risk gene for hereditary spastic paraplegia. Furthermore, de novo missense mutations in TOMM70 have been identified to cause neurological impairments in two unrelated patients. Here, we show that mutant zebrafish ruehreip25ca also harbor a missense mutation in tomm70, affecting the same conserved isoleucine residue as in one of the human patients. Using this model, we demonstrate how loss of Tomm70 function leads to impairment. At the molecular level, the mutation affects the interaction of Tomm70 with the endoplasmic reticulum protein Lam6, a known sterol transporter. At the neuronal level, the mutation impairs mitochondrial transport to the axons and dendrites, leading to demyelination of large calibre axons in the spinal cord. These neurodegenerative defects in zebrafish are associated with reduced endurance, swimming efficiency, and alterations in the C-start escape response, which correlate with decreased spiking in giant Mauthner neurons. Thus, in zebrafish, a mutation in the endoplasmic reticulum-mitochondria contact site protein Tomm70 recreates some of the neurodegenerative phenotypes characteristic of hereditary spastic paraplegia.© 2025. Published by The Company of Biologists.
Renal Implications of Dysregulated Protein Homeostasis: Insights into Ubiquitin-Proteasome and Autophagy Systems
Delrue, Speeckaert
Biomolecules (2025) 15 (3)
Abstract: The ubiquitin-proteasome system (UPS) and autophagy maintain protein homeostasis, which is critical to cellular function and survival. The dysregulation of these pathways has been recognized as a hallmark of acute kidney injury and chronic kidney disease. This review elucidates the role of the UPS and autophagy in kidney disease, namely through inflammation, oxidative stress, fibrosis and apoptosis. The pathways of NF-κB, TGF-β and mitochondrial failure result in glomerular injury and tubulointerstitial fibrosis due to impaired proteostasis in podocytes and tubular epithelial cells. Recent studies have revealed a connection between the autophagic process and the UPS, wherein compensatory mechanisms aim to spike down proteotoxic stress but eventually seem inadequate in cases of chronic derangement. Low-dose pharmacological inhibitors, autophagy modulators, and new gene and nanotechnology-based treatments may all help to restore the protein balance and reduce kidney injury. A more thorough understanding of these pathways is needed to develop kidney-protective and disease-modifying therapeutic interventions.
Showing 1-4 of 39023 papers.
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