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AB273074

Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric)

4

(9 Reviews)

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(10 Publications)

Rabbit Recombinant Monoclonal SPIKE antibody. Suitable for ELISA, I-ELISA and reacts with Recombinant full length protein - SARS-CoV-2, Recombinant full length protein - SARS-CoV samples. Cited in 10 publications. Immunogen corresponding to Cell preparation containing SARS-CoV-2 Spike Glycoprotein S1 protein.

View Alternative Names

2, S, Spike glycoprotein, S glycoprotein, E2, Peplomer protein

6 Images
ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)
  • ELISA

Supplier Data

ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)

Binding curve of ab273073 to SARS-CoV-2 Spike Glycoprotein (S1), Sheep Fc-Tag and SARS-CoV-2 Spike Glycoprotein (S2), Sheep Fc-Tag from HEK293 cells.

ELISA plate coated with SARS-CoV-2 Spike Glycoprotein (S1), Sheep Fc-Tag (blue line) or SARS-CoV-2 Spike Glycoprotein (S2), Sheep Fc-Tag (orange line) from HEK293 cells at concentrations of 5 μg/ml. A 3-fold serial dilution from 125 ng/ml was performed using ab273073.

For detection, a 1/4000 dilution of HRP-labelled anti-human IgG antibody was used.

This data was developed using an alternative version of this antibody clone (ab272073).

ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)
  • ELISA

Supplier Data

ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)

Binding curve of ab273073 to SARS-CoV-2 Spike Glycoprotein domains S1 and S2 of various origin.

ELISA plate coated with SARS-CoV-2 Spike Glycoprotein (S1), His-Tag (Insect Cells; grey line), SARS-CoV-2 Spike Glycoprotein (S2), His-Tag (Insect Cells; yellow line) and SARS Coronavirus Spike Glycoprotein (S1), His-Tag (HEK293 cells; blue line) at concentrations of 5 μg/ml. A 3-fold serial dilution from 41.6 ng/ml was performed using ab273073.

For detection, a 1/4000 dilution of HRP-labelled anti-human IgG antibody was used.

This data was developed using an alternative version of this antibody clone (ab272073).

Indirect ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)
  • I-ELISA

Lab

Indirect ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)

Indirect ELISA showing primary antibody ab273074 (CR3022, rabbit chimeric) binding to the antigen ab273068 (recombinant human coronavirus SARS-CoV-2 Spike Glycoprotein S1 (Active)). Plates were coated with 100ng/well ab272105 or ab273068 and binding of ab273073 assessed in serial dilution from 200ng/ml primary antibody in duplicate. Binding was detected using ab97080, an anti-rabbit H&L secondary conjugated to HRP. Data are represented as the mean and error bars represent standard deviation.

ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)
  • ELISA

Lab

ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)

Plates were coated with Recombinant Human coronavirus SARS-CoV-2 Spike Glycoprotein S1 (Fc Chimera, ab272105) or Recombinant Human coronavirus SARS-CoV-2 Spike Glycoprotein S2 (Fc Chimera, ab272106) at 1000 ng/ml at 1000 ng/ml.
Primary antibody (ab273074) concentration range 0.045-100 ng /ml.
Pre-adsorbed secondary antibody, goat anti-rabbit IgG H&L (HRP, ab97080) used at 1/2000 dilution.

ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)
  • ELISA

Unknown

ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)

ELISA using ab273073 and mutant spike proteins. The plate was coated with the mutant spike protein variants (The Native Antigen Company) at 2.5 μg/ml. ab01680 was conjugated to HRP and titrated on a 3-fold serial dilution starting at 1,000 ng/ml. CR3022 (ab01680) exhibited exceptional binding to all mutant spike proteins. RBD WT – wild-type receptor binding domain.

ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)
  • ELISA

Unknown

ELISA - Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody [CR3022] - Rabbit IgG (Chimeric) (AB273074)

ELISA using ab273073 with UK (B.1.1.7) and South African (B.1.351 (501Y.V2)) mutant spike proteins. The plate was coated with the mutant spike protein variants (The Native Antigen Company) at 2.5 μg/ml. ab01680 was conjugated to HRP and titrated on a 3-fold serial dilution starting at 1,000 ng/ml. CR3022 (ab01680) exhibited exceptional binding to all mutant spike proteins. WT – wild type.

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

CR3022

Isotype

IgG

Light chain type

kappa

Carrier free

No

Reacts with

SARS-CoV-2, SARS-CoV

Applications

I-ELISA, ELISA

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Epitope

This antibody binds the amino acids 318-510 in the S1 domain of the SARS-CoV Spike protein as well as SARS-CoV-2 (COVID-19) Spike protein. The antibody also binds to P462L-substituted S318–510 fragments of the SARS spike protein. The binding epitope is only accessible in the "open" conformation of the spike protein (Joyce et al. 2020)

Reactivity data

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Product details

This rabbit monoclonal chimeric antibody was made using the variable domain sequences of the original Human IgG1 format, for improved compatibility with existing reagents, assays and techniques.

The original CR3022 antibody was generated by sequencing peripheral blood lymphocytes of a patient exposed to the SARS-CoV. This antibody was shown to neutralize SARS-COV in a concerted action with clone CR3014. Presence of both antibodies delivers a blocking action of the SARS-COV RBD-ACE2 interaction, by binding two distinct and functional epitopes (16796401).

CR3022 has been shown to bind with a high affinity to SARS-CoV2 (32416259, 32413276). Structural modelling has confirmed that CR3022 targets a conserved epitope between SARS-CoV and SARS-CoV2 in the RBD domain (32245784, 32065055). Precisely, this antibody binds to the 'open' conformation of the spike protein to the amino acids 318-510 in the S1 domain of the SARS-CoV as well as SARS-CoV-2 strains (32245784, Joyce et al. 2020). The antibody is also able to bind the P462L-substituted S318–510 fragments of the SARS spike protein. The binding epitope of clone CR3022 does not overlap with the ACE2 binding site of SARS-COV2 (32065055). Therefore whilst CR3022 can neutralise SARS-COV in in a concerted action with clone CR3014, CR3022 is not believed to independently neutralise SARS-COV2, based on in vitro studies (32226289, 32065055, 32383254, 32416259).

Recombinant Anti-SARS-CoV-2 Spike Glycoprotein S1 antibody (ab273074) is a Rabbit Chimeric version of CR3022 for research use only. CR3022 is also available as a human monoclonal antibody (ab273073).

Applications overview

Tick: Tested and Guaranteed to work X: Will not work —: No data

<img src="https://www.abcam.com/ps/Products/273/ab273074/Images/ab273074-394520-ab273074-applications-overview.jpg" height="123" width="674">

ab273074 was developed to have a rabbit IgG isotype.
Other isotypes of clone CR3022 available:
ab278112 – human IgA
ab273073 – human IgG1
ab278111 – human IgM
ab273886 – rat IgG2a

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
Preservative: 0.02% Proclin 300 Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The SARS-CoV-2 Spike Glycoprotein S1 also known as the G10 spike or glycoprotein spike plays an important role in allowing the virus to attach and enter host cells. This protein with a mass of approximately 180 kDa is located on the surface of the virus and forms the outer spikes observed in coronaviruses. Expression of the spike glycoprotein is in virus-infected cells where it facilitates the interaction with host cell receptors. The S1 subunit includes a receptor-binding domain that specifically binds to the human angiotensin-converting enzyme 2 (ACE2) receptors initiating the infection process.
Biological function summary

The spike glycoprotein S1 mediates the fusion of the viral and cellular membranes which is necessary for viral entry. It forms part of a larger trimeric complex comprising S1 and S2 subunits. This complex undergoes conformational changes that drive the membrane fusion process. The glycoprotein contains multiple glycosylation sites which help shield the virus from the host immune response. The proper function and presentation of this glycoprotein are critical for efficient viral spread and infection establishment.

Pathways

The spike glycoprotein S1 is integral to the viral infection pathway and host immune evasion. It interacts with the renin-angiotensin system by binding to the ACE2 receptor disrupting normal receptor activity. This interaction not only facilitates viral entry but also impacts the homeostatic functions typically mediated by ACE2 which include blood pressure regulation. Additionally the spike protein is involved in downstream activation of immune signaling pathways including those related to inflammation and cytokine production which may involve proteins such as IL-6.

Infection with the spike glycoprotein S1 is directly related to COVID-19. The binding to ACE2 receptors is linked to the pathology of the disease contributing to respiratory symptoms and in severe cases acute respiratory distress syndrome (ARDS). Through the IL-6 signaling pathway the spike protein is indirectly connected to cytokine release syndrome often observed in severe COVID-19 cases. This connection highlights the importance of targeting this glycoprotein for potential therapeutic interventions and diagnostics such as ELISA SARS-CoV-2 tests and the development of anti-spike antibodies available on platforms like antispark.com for research and clinical purposes.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Spike protein S1. Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. The major receptor is host ACE2 (PubMed : 32142651, PubMed : 32155444, PubMed : 33607086). When S2/S2' has been cleaved, binding to the receptor triggers direct fusion at the cell membrane (PubMed : 34561887). When S2/S2' has not been cleaved, binding to the receptor results in internalization of the virus by endocytosis using host TFRC and GRM2 and leading to fusion of the virion membrane with the host endosomal membrane (PubMed : 32075877, PubMed : 32221306, PubMed : 34903715, PubMed : 36779763). Alternatively, may use NRP1/NRP2 (PubMed : 33082294, PubMed : 33082293) and integrin as entry receptors (PubMed : 35150743). The use of NRP1/NRP2 receptors may explain the tropism of the virus in human olfactory epithelial cells, which express these molecules at high levels but ACE2 at low levels (PubMed : 33082293). Uses also ASGR1 as an alternative receptor in an ACE2-independent manner (PubMed : 34837059). The stalk domain of S contains three hinges, giving the head unexpected orientational freedom (PubMed : 32817270).. Spike protein S2. Precursor of the fusion protein processed in the biosynthesis of the S protein and the formation of virus particle. Mediates fusion of the virion and cellular membranes by functioning as a class I viral fusion protein. Contains two viral fusion peptides that are unmasked after cleavage. The S2/S2' cleavage occurs during virus entry at the cell membrane by host TMPRSS2 (PubMed : 32142651) or during endocytosis by host CSTL (PubMed : 32703818, PubMed : 34159616). In either case, this triggers an extensive and irreversible conformational change leading to fusion of the viral envelope with the cellular cytoplasmic membrane, releasing viral genomic RNA into the host cell cytoplasm (PubMed : 34561887). 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 fusion of the viral and target cell membranes, the coiled coil regions (heptad repeats) adopt a trimer-of-hairpins structure and position the fusion peptide in close proximity to the C-terminal region of the ectodomain. Formation of this structure appears to promote apposition and subsequent fusion of viral and target cell membranes.. Spike protein S2'. Subunit of the fusion protein that is processed upon entry into the host cell. Mediates fusion of the virion and cellular membranes by functioning as a class I viral fusion protein. Contains a viral fusion peptide that is unmasked after S2 cleavage. This cleavage can occur at the cell membrane by host TMPRSS2 or during endocytosis by host CSTL (PubMed : 32703818, PubMed : 34159616). In either case, this triggers an extensive and irreversible conformational change that leads to fusion of the viral envelope with the cellular cytoplasmic membrane, releasing viral genomic RNA into the host cell cytoplasm (PubMed : 34561887). 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 fusion of the viral and target cell membranes, the coiled coil regions (heptad repeats) adopt a trimer-of-hairpins structure and position the fusion peptide in close proximity to the C-terminal region of the ectodomain. Formation of this structure appears to promote apposition and subsequent fusion of viral and target cell membranes.
See full target information S

Publications (10)

Recent publications for all applications. Explore the full list and refine your search

ACS sensors 10:1407-1418 PubMed39960416

2025

Using Machine Learning and Optical Microscopy Image Analysis of Immunosensors Made on Plasmonic Substrates: Application to Detect the SARS-CoV-2 Virus.

Applications

Unspecified application

Species

Unspecified reactive species

Pedro R A Oiticica,Monara K S C Angelim,Juliana C Soares,Andrey C Soares,José L Proença-Módena,Odemir M Bruno,Osvaldo N Oliveira

Biomedicines 11: PubMed38137414

2023

Application of a Receptor-Binding-Domain-Based Simple Immunoassay for Assessing Humoral Immunity against Emerging SARS-CoV-2 Virus Variants.

Applications

Unspecified application

Species

Unspecified reactive species

Orsolya Mózner,Judit Moldvay,Kata Sára Szabó,Dorottya Vaskó,Júlia Domján,Dorottya Ács,Zoltán Ligeti,Csaba Fehér,Edit Hirsch,László Puskás,Cordula Stahl,Manfred Frey,Balázs Sarkadi

Biosensors & bioelectronics: X 11:100167 PubMed35647519

2022

Evaluation of a photoelectrochemical platform based on strontium titanate, sulfur doped carbon nitride and palladium nanoparticles for detection of SARS-CoV-2 spike glycoprotein S1.

Applications

Unspecified application

Species

Unspecified reactive species

Chirlene N Botelho,Suringo S Falcão,Rossy-Eric P Soares,Silma R Pereira,Alan S de Menezes,Lauro T Kubota,Flavio S Damos,Rita C S Luz

iScience 24:103295 PubMed34693218

2021

Effective chimeric antigen receptor T cells against SARS-CoV-2.

Applications

Unspecified application

Species

Unspecified reactive species

Xueyang Guo,Alexandra Kazanova,Stephanie Thurmond,H Uri Saragovi,Christopher E Rudd

Biocontrol science 26:119-125 PubMed34092715

2021

Effect of the Photocatalyst under Visible Light Irradiation in SARS-CoV-2 Stability on an Abiotic Surface.

Applications

Unspecified application

Species

Unspecified reactive species

Masashi Uema,Kenzo Yonemitsu,Yoshika Momose,Yoshikazu Ishii,Kazuhiro Tateda,Takao Inoue,Hiroshi Asakura

Biosensors & bioelectronics 180:113122 PubMed33706157

2021

SARS-CoV-2 S1 NanoBiT: A nanoluciferase complementation-based biosensor to rapidly probe SARS-CoV-2 receptor recognition.

Applications

Unspecified application

Species

Unspecified reactive species

Taha Azad,Ragunath Singaravelu,Emily E F Fekete,Zaid Taha,Reza Rezaei,Rozanne Arulanandam,Stephen Boulton,Jean-Simon Diallo,Carolina S Ilkow,John C Bell

Analytical and bioanalytical chemistry 414:103-113 PubMed33616686

2021

The role of the surface ligand on the performance of electrochemical SARS-CoV-2 antigen biosensors.

Applications

Unspecified application

Species

Unspecified reactive species

Sabine Szunerits,Quentin Pagneux,Abir Swaidan,Vladyslav Mishyn,Alain Roussel,Christian Cambillau,David Devos,Ilka Engelmann,Enagnon Kazali Alidjinou,Henri Happy,Rabah Boukherroub

Molecular therapy : the journal of the American Society of Gene Therapy 29:1984-2000 PubMed33578036

2021

Nanoluciferase complementation-based bioreporter reveals the importance of N-linked glycosylation of SARS-CoV-2 S for viral entry.

Applications

Unspecified application

Species

Unspecified reactive species

Taha Azad,Ragunath Singaravelu,Zaid Taha,Taylor R Jamieson,Stephen Boulton,Mathieu J F Crupi,Nikolas T Martin,Emily E F Fekete,Joanna Poutou,Mina Ghahremani,Adrian Pelin,Kazem Nouri,Reza Rezaei,Christopher Boyd Marshall,Masahiro Enomoto,Rozanne Arulanandam,Nouf Alluqmani,Reuben Samson,Anne-Claude Gingras,D William Cameron,Peter A Greer,Carolina S Ilkow,Jean-Simon Diallo,John C Bell

Emerging microbes & infections 9:382-385 PubMed32065055

2020

Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaolong Tian,Cheng Li,Ailing Huang,Shuai Xia,Sicong Lu,Zhengli Shi,Lu Lu,Shibo Jiang,Zhenlin Yang,Yanling Wu,Tianlei Ying

PLoS medicine 3:e237 PubMed16796401

2006

Human monoclonal antibody combination against SARS coronavirus: synergy and coverage of escape mutants.

Applications

Unspecified application

Species

Unspecified reactive species

Jan ter Meulen,Edward N van den Brink,Leo L M Poon,Wilfred E Marissen,Cynthia S W Leung,Freek Cox,Chung Y Cheung,Arjen Q Bakker,Johannes A Bogaards,Els van Deventer,Wolfgang Preiser,Hans Wilhelm Doerr,Vincent T Chow,John de Kruif,Joseph S M Peiris,Jaap Goudsmit
View all publications

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