S Recombinant Monoclonal Antibody

Code: CSB-RA33245A1GMY

Rate （5.0）
Review （1）
Citation （1）

Size:

50ul100ul

US$210

Quantity:

Species Reactivity: Human Novel Coronavirus (SARS-CoV-2/ 2019-nCoV)

Application: ELISA, GICA, Neutralising

Send an Inquiry

Start an on-line Chat

Online ordering is currently available for U.S. customers only. For orders outside the U.S., please kindly submit an inquiry or start a chat with us.

Product Details
Related Products
Customer Reviews and Q&A
Target Background

Product Details

Uniprot NO.

P0DTC2

Alternative Names

S; 2; Spike glycoprotein; S glycoprotein; E2; Peplomer protein)

Species Reactivity

Human Novel Coronavirus (SARS-CoV-2/ 2019-nCoV)

Immunogen

Recombinant Human Novel Coronavirus Spike glycoprotein (S) (16-685aa) (CSB-MP3324GMY)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Mouse scFv fusion with human IgG1 Fc

Clone No.

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4

Form

Liquid
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Scope Application

ELISA Protocol

Recommended Dilution

Application	Recommended Dilution
ELISA	1:10000-1:50000
GICA	1:500-1:5000
Neutralising	1:50-1:10000

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Datasheet & COA

Antibody FAQs

Images

The Binding Activity of SARS-CoV-2-S Antibody with SARS-CoV-2-S
Activity: Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-S (CSB-MP3324GMY) at 2 μg/ml can bind SARS-CoV-2-S Antibody, the EC₅₀ is 42.83 ng/ml.
The Binding Activity of SARS-CoV-2-S Antibody with SARS-CoV-2-S1-RBD
Activity: Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-S1-RBD (CSB-YP3324GMY1) at 2 μg/ml can bind SARS-CoV-2-S Antibody, the EC₅₀ is 29.51 ng/ml.
In the Colloidal Gold Immunochromatography Assay detection system, the background of antibody (CSB-RA33245A1GMY) is clean, the detection limit can be as low as 223.2ng/ml (15.625ng/0.07ml), and the sensitivity is very good.
Binding signal of SARS-CoV-2-S1-RBD (CSB-YP3324GMY1) and ACE2 protein-HRP conjugate (CSB-MP866317HU) was inhibited by S Antibody (CSB-RA33245A1GMY) with the IC₅₀ is 23.32 nM.
Binding signal of SARS-CoV-2-S1-RBD (CSB-YP3324GMY1) and ACE2 protein-HRP conjugate (CSB-MP866317HU) was inhibited by S Antibody (CSB-RA33245A1GMY) with the IC₅₀ is 2.38 μg/ml.
ELISA: Immobilize various types of SARS proteins at concentration of 2μg/ml on solid substrate, then react with SARS-CoV-2-S Antibody at concentration of 100μg/ml, 10μg/ml and 1μg/ml. It shows the SARS-CoV-2-S Antibody (CSB-RA33245A1GMY) is specific for SARS-CoV-2-S1-RBD protein, without any cross-reactivity with MERS-CoV, SARS-CoV, HCoV-OC43 or HCoV-229E.
The Binding Activity of S protein with S Recombinant Antibody. Activity: Measured by its binding ability in a functional ELISA. Immobilized S at 2 μg/ml can bind S Recombinant Antibody, the EC₅₀ of S Recombinant Antibody.
The Binding Activity of S protein with S Recombinant Antibody. Activity: Measured by its binding ability in a functional ELISA. Immobilized S at 2 μg/ml can bind S Recombinant Antibody, the EC₅₀ of S Recombinant Antibody.
The Binding Activity of S protein with S Recombinant Antibody. Activity: Measured by its binding ability in a functional ELISA. Immobilized S at 2 μg/ml can bind S Recombinant Antibody, the EC₅₀ of S Recombinant Antibody. The Binding Activity of S protein with S Recombinant Antibody. Activity: Measured by its binding ability in a functional ELISA. Immobilized S at 2 μg/ml can bind S.
The Binding Activity of S protein with S Recombinant Antibody. Activity: Measured by its binding ability in a functional ELISA. Immobilized S at 2 μg/ml can bind S Recombinant Antibody, the EC₅₀ of S Recombinant Antibody.

Description

The SARS-CoV-2 spike glycoprotein serves as the primary mediator of viral entry into host cells, making it a central focus for researchers studying coronavirus biology, vaccine development, and therapeutic interventions. The receptor-binding domain within the S1 subunit directly engages human ACE2, establishing this protein as a critical target for neutralization studies and diagnostic assay development.

This recombinant monoclonal antibody, clone H6, offers researchers the reproducibility essential for longitudinal studies and multi-site collaborations. As a sequence-defined reagent produced through recombinant technology, it eliminates the lot-to-lot variability inherent in traditional hybridoma-derived antibodies, ensuring your experimental conditions remain consistent across projects.

Functional validation demonstrates robust binding characteristics, with EC50 values of 42.83 ng/ml against the full spike protein and 29.51 ng/ml against the S1-RBD specifically. Importantly, this antibody exhibits genuine neutralizing capability, blocking the spike-ACE2 interaction with an IC50 of 23.32 nM, making it suitable for functional studies examining viral entry mechanisms. Specificity testing confirms reactivity is restricted to SARS-CoV-2, with no cross-reactivity observed against MERS-CoV, SARS-CoV, HCoV-OC43, or HCoV-229E spike proteins—a valuable characteristic when distinguishing between coronavirus strains in your research.

The antibody performs across multiple platforms, including ELISA at dilutions from 1:10,000 to 1:50,000, colloidal gold immunochromatography assays with detection limits as low as 223.2 ng/ml, and neutralization assays. This versatility supports workflows ranging from quantitative binding studies to rapid diagnostic development. The scFv-human IgG1 Fc fusion format combines the specificity of a defined binding domain with the stability and detection compatibility of a human constant region, supporting diverse downstream applications in infectious disease research.

Customer Reviews and Q&A

■ Customer Reviews

Average Rating:

5.0 - 1 reviews

Submit a Review here

Applications : Fabrication of MO CM Biochips

Sample type: magneto-optical biochip

Review: the antibody of spike glycoprotein (anti-S, 10 μg/mL, 40 μL) was added and conjugated with GA. Te absorption peaks of the biochip after the fabrication process of Au nanostructure, APTMS, GA and BSA are 532 nm, 537 nm, 538 nm and 547 nm, respectively.

By Anonymous

Citations

A magneto-optical biochip for rapid assay based on the Cotton–Mouton effect of γ-Fe2O3@ Au core/shell nanoparticles KL Chen,/,2021

Target Background

Function(From Uniprot)

attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein. Binding to host NRP1 and NRP2 via C-terminal polybasic sequence enhances virion entry into host cell. This interaction may explain virus tropism of human olfactory epithelium cells, which express high level of NRP1 and NRP2 but low level of ACE2. The stalk domain of S contains three hinges, giving the head unexpected orientational freedom. Uses human TMPRSS2 for priming in human lung cells which is an essential step for viral entry. Can be alternatively processed by host furin. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.; mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.; Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.; May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity.

Gene References into Functions

Study presents crystal structure of C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike S protein in complex with human ACE2 (hACE2); hACE2-binding mode similar overall to that observed for SARS-CoV. However, details at the binding interface show that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-CoV receptor-binding domain. PMID:32378705
crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2 PMID:32365751
crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2 PMID:32320687
Out of the two isolates from India compared to the isolates from Wuhan, China, one was found to harbor a mutation in its receptor-binding domain (RBD) at position 407 where, arginine was replaced by isoleucine. This mutation has been seen to change the secondary structure of the protein at that region and this can potentially alter receptor binding of the virus. PMID:32275855
Structural modeling of the SARS-CoV-2 spike glycoprotein show similar receptor utilization between SARS-CoV-2 and SARS-CoV, despite a relatively low amino acid similarity in the receptor binding module. Compared to SARS-CoV and all other coronaviruses in Betacoronavirus lineage B, an extended structural loop containing basic amino acids were identified at the interface of the receptor binding (S1) and fusion (S2) domains. PMID:32245784
crystal structure of CR3022, a neutralizing antibody from a SARS patient, in complex with the receptor-binding domain of the SARS-CoV-2 spike (S) protein to 3.1 A; study provides insight into how SARS-CoV-2 can be targeted by the humoral immune response and revealed a conserved, but cryptic epitope shared between SARS-CoV-2 and SARS-CoV PMID:32225176
SARS-CoV and SARS-CoV-2 spike proteins have comparable binding affinities achieved by balancing energetics and dynamics. The SARS-CoV-2-ACE2 complex contains a higher number of contacts, a larger interface area, and decreased interface residue fluctuations relative to the SARS-CoV-ACE2 complex. PMID:32225175
Interaction interface between cat/dog/pangolin/Chinese hamster ACE2 and SARS-CoV/SARS-CoV-2 S protein was simulated through homology modeling. Authors identified that N82 of ACE2 showed closer contact with receptor-binding domain of S protein than human ACE2. PMID:32221306
SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs; determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer. PMID:32201080
Study demonstrates that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. PMID:32155444
The ACE2-B0AT1 complex exists as a dimer of heterodimers. Structural alignment of the RBD-ACE2-B0AT1 ternary complex with the S protein of SARS-CoV-2 suggests that two S protein trimers can simultaneously bind to an ACE2 homodimer. PMID:32142651
study demonstrated SARS-CoV-2 S protein entry on 293/hACE2 cells is mainly mediated through endocytosis, and PIKfyve, TPC2 and cathepsin L are critical for virus entry; found that SARS-CoV-2 S protein could trigger syncytia in 293/hACE2 cells independent of exogenous protease; there was limited cross-neutralization activity between convalescent sera from SARS and COVID-19 patients PMID:32132184
study determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation; provided biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S PMID:32075877

Hide All

Subcellular Location

Virion membrane; Single-pass type I membrane protein. Host endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein.

Protein Families

Betacoronaviruses spike protein family

Promotions