SARS-CoV-2 (2019-nCoV) Spike S1 Antibody, Rabbit MAb sinobiological 40150-R007

$114.00
In stock
SKU
40150-R007
Catalog No.SizePrice (USD)
40150-R007-2020 µL$118.49
40150-R007-5050 µL$222.17
40150-R007-100100 µL$370.28

General Information

Product nameSARS-CoV-2 (2019-nCoV) Spike S1 Antibody, Rabbit MAb
Validated applicationsELISA (FAQ Protocol)
Application notesIHC, FCM, IF, IP et al. applications haven't been validated. (Antibody's applications haven't been validated with corresponding virus positive samples. Optimal concentrations/dilutions should be determined by the end user.)
SpecificitySARS-CoV-2 Spike S1 Protein SARS-CoV-2 Spike RBD Protein SARS-CoV Spike S1 Protein SARS-CoV Spike RBD Protein Has cross-reactivity in ELISA with SARS-CoV-2 Omicron (LP.8.1) Spike S1+S2 trimer Protein (Cat# 40589-V08H69) SARS-CoV-2 Omicron (KP.3.1.1) Spike S1+S2 trimer Protein (Cat# 40589-V08H63) SARS-COV-2 Omicron (KP.3) Spike S1+S2 trimer Protein (Cat# 40589-V08H64) SARS-CoV-2 (LP.8.1) Spike RBD Protein (Cat# 40592-V08H160) SARS-CoV-2 (LF.7) Spike RBD Protein (Cat# 40592-V08H159) SARS-CoV-2 (XEC) Spike S1+S2 trimer Protein (Cat# 40589-V08H62) SARS-COV-2 Omicron (KP.2) Spike S1+S2 trimer Protein (Cat# 40589-V08H61) SARS-COV-2 Omicron (KP.2) Spike RBD Protein (Cat# 40592-V08H156) SARS-COV-2 Omicron (KP.3) Spike RBD Protein (Cat# 40592-V08H157) SARS-CoV-2 Omicron (XBB.1.16) Spike S1+S2 trimer Protein (Cat# 40589-V08H48) SARS-CoV-2 Omicron (XBB.1.5) Spike RBD Protein (Cat# 40592-V08H146) SARS-CoV-2 Omicron (XBB.1.5) Spike S1+S2 trimer Protein (Cat# 40589-V08H45) SARS-CoV-2 Omicron (XBB.1) Spike S1+S2 trimer Protein (Cat# 40589-V08H42) SARS-CoV-2 Omicron (XBB) Spike RBD Protein (Cat# 40592-V08H144) SARS-CoV-2 Omicron (BQ.1.1) Spike S1+S2 trimer Protein (Cat# 40589-V08H41) SARS-CoV-2 Omicron (BQ.1.1) Spike RBD Protein (Cat# 40592-V08H143) SARS-CoV-2 Omicron (BF.7) Spike S1+S2 trimer Protein (Cat# 40589-V08H39) SARS-CoV-2 Omicron (BA.4.6/BF.7) Spike RBD Protein (Cat# 40592-V08H140) SARS-CoV-2 Omicron (BA.4.6) Spike S1+S2 trimer Protein (Cat# 40589-V08H37) SARS-CoV-2 Omicron (BA.2.75) Spike RBD Protein (Cat# 40592-V08H135) SARS-CoV-2 Omicron (BA.2.75) Spike S1+S2 trimer Protein (Cat# 40589-V08H36) SARS-CoV-2 Omicron (BA.2.75.2) Spike RBD Protein (Cat# 40592-V08H141) SARS-CoV-2 Omicron (BA.2.75.2) Spike S1+S2 trimer Protein (Cat# 40589-V08H38) SARS-CoV-2 Omicron (BA.2.3.20) Spike RBD Protein (Cat# 40592-V08H142) SARS-CoV-2 Omicron (BA.1.1) Spike S1+S2 trimer Protein (Cat# 40589-V08H29) SARS-CoV-2 Omicron (BA.1.1) Spike RBD Protein (Cat# 40592-V08H129) SARS-CoV-2 Omicron (B.1.1.529) S1+S2 trimer Protein (Cat# 40589-V08H26) SARS-CoV-2 Omicron (B.1.1.529) Spike S1 Protein (Cat# 40591-V08H41) SARS-CoV-2 Omicron (B.1.1.529) Spike RBD Protein (Cat# 40592-V08H121) SARS-CoV-2 Omicron (BA.2) Spike S1+S2 trimer Protein (Cat# 40589-V08H28) SARS-CoV-2 Omicron (BA.2) Spike S1 Protein (Cat# 40591-V08H43) SARS-CoV-2 Omicron (BA.2) Spike RBD Protein (Cat# 40592-V08H123) SARS-CoV-2 Omicron (BA.2.12.1) Spike RBD Protein (Cat# 40592-V08H132) SARS-CoV-2 Omicron (BA.4) Spike RBD Protein (Cat# 40592-V08H130) SARS-CoV-2 XD(BA.1 x AY.4) Spike S1+S2 trimer Protein (Cat# 40589-V08H30) SARS-CoV-2 Delta (B.1.617.2) Spike S1+S2 trimer Protein (Cat# 40589-V08H10) SARS-CoV-2 Delta (B.1.617.2) Spike S1+S2 Protein (Cat# 40589-V08B16) SARS-CoV-2 Delta (B.1.617.2) Spike S1 Protein (Cat# 40591-V08H23) SARS-CoV-2 Delta (B.1.617.2) Spike RBD Protein (Cat# 40592-V08H90) SARS-CoV-2 Spike S1 Protein (Cat# 40591-V08H) Medium cross-reactivity in ELISA with SARS-CoV-2 Omicron (BA.5) Spike RBD Protein (Cat# 40592-V08H131) No cross-reactivity in ELISA with SARS-CoV-2 Omicron (BA.2) Spike S1 NTD Protein (Cat# 40591-V08H44) SARS-CoV-2 Delta (B.1.617.2) Spike S1 NTD Protein (Cat# 40591-V08H36) MERS-CoV Spike S1 Protein (Cat# 40069-V08B1) HCoV-HKU1 (isolate N1) Spike S1 Protein (Cat# 40021-V08H) HCoV-HKU1 (isolate N5) Spike S1 Protein (Cat# 40602-V08H) HCoV-NL63 Spike S1 Protein (Cat# 40600-V08H) HCoV-229E Spike S1 Protein (Cat# 40601-V08H) HCoV-OC43 Spike S1+S2 ECD Protein (Cat# 40607-V08B)
ImmunogenRecombinant SARS-CoV Spike S1 Subunit Protein (Catalog#40150-V08B1)
PreparationThis product is a recombinant monoclonal antibody expressed from HEK293 cells.
SourceMonoclonal Rabbit IgG Clone #007
PurificationProtein A
Formulation0.2 μm filtered solution in PBS
ConjugateUnconjugated
FormLiquid
ShippingThis antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
StorageThis antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.

Image / Experimental Information

Image 1 DescriptionImmunofluorescence staining of SARS-CoV-2 (2019-nCoV) Spike in ACE2-overexpressed 293T cells, infected (left) or noninfected (right) by 2019-nCOV-Spike pseudovirus (PSV). Cells were blocked with 10% serum, and incubated with SARS-CoV-2 (2019-nCoV) Spike rabbit monoclonal antibody (dilution ratio 1:60) at 37℃ for 1 hour. Then cells were stained with the Alexa Fluor®-conjugated Goat Anti-rabbit IgG secondary antibody (green). (Validation Experiment)
Image 1 Alt Text2019-nCoV CoV spike Immunofluorescence(IF) 29827
Image 1 URLSource image

Background Information

DescriptionThe spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2 (angiotensin-converting enzyme 2), DPP4 (dipeptidyl peptidase-4), APN (aminopeptidase N), CEACAM (carcinoembryonic antigen-related cell adhesion molecule), Sia (sialic acid), O-ac Sia (O-acetylated sialic acid). The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 2019-nCoV) 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
References
  1. Shen S, et al . (2007) Expression, glycosylation, and modification of the spike (S) glycoprotein of SARS CoV. Methods Mol Biol. 379: 127-35.
  2. Du L, et al . (2009) The spike protein of SARS-CoV--a target for vaccine and therapeutic development. Nat Rev Microbiol. 7 (3): 226-36.
  3. Xiao X, et al . (2004) The SARS-CoV S glycoprotein. Cell Mol Life Sci. 61 (19-20): 2428-30.

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A randomised controlled trial","authors":["D.W. Seymour","G. Forshaw","...","P.J. Nixon"],"journal":"Access Microbiology","date":"2024-01-01","pmid":"","doi":"10.1099/acmi.0.000722.v3"},{"title":"Responses of primary human nasal epithelial cells to COVID-19 vaccine candidate","authors":[],"journal":"Asian Pacific Journal of Allergy and Immunology","date":"2024-01-01","pmid":"","doi":"10.12932/ap-230523-1623"},{"title":"A Point-of-Care Testing Device Utilizing Graphene-Enhanced Fiber Optic SPR Sensor for Real-Time Detection of Infectious Pathogens","authors":["Shiyu Jiang","Siyu Qian","...","Shengchun Liu"],"journal":"Biosensors","date":"2023-12-14","pmid":"38131789","doi":""},{"title":"Drug repurposing for the treatment of COVID-19: Targeting nafamostat to the lungs by a liposomal delivery system.","authors":["Philipp Reus","Hadar Guthmann","...","Gershon Golomb"],"journal":"Journal of controlled release : official journal of the Controlled Release Society","date":"2023-12-05","pmid":"37939853","doi":"10.1016/j.jconrel.2023.10.050"},{"title":"An FcRn-targeted mucosal vaccine against SARS-CoV-2 infection and transmission.","authors":["Weizhong Li","Tao Wang","...","Xiaoping Zhu"],"journal":"Nature Communications","date":"2023-11-28","pmid":"37932271","doi":""},{"title":"Wireless, battery-free, multifunctional integrated bioelectronics for respiratory pathogens monitoring and severity evaluation","authors":["Hu Li","Huarui Gong","...","Xinge Yu"],"journal":"Nature Communications","date":"2023-11-20","pmid":"37985765","doi":""},{"title":"The Apolipoprotein E neutralizing antibody inhibits SARS‐CoV‐2 infection by blocking cellular entry of lipoviral particles","authors":["Qi Cui","Arjit Vijey Jeyachandran","...","Yanhong Shi"],"journal":"MedComm","date":"2023-10-10","pmid":"","doi":"10.1002/mco2.400"},{"title":"SARS-CoV-2 Omicron entry is type II transmembrane serine protease-mediated in human airway and intestinal organoid models.","authors":["Anna Z Mykytyn","Tim I Breugem","...","Mart M Lamers"],"journal":"Journal of virology","date":"2023-09-06","pmid":"37555660","doi":"10.1128/jvi.00851-23"},{"title":"Oral Immunization with rVSV Bivalent Vaccine Elicits Protective Immune Responses, Including ADCC, against Both SARS-CoV-2 and Influenza A Viruses.","authors":["Maggie Jing Ouyang","Zhujun Ao","...","Xiaojian Yao"],"journal":"Vaccines","date":"2023-08-23","pmid":"37766083","doi":"10.3390/vaccines11091404"},{"title":"In vivo inhibition of nuclear ACE2 translocation protects against SARS-CoV-2 replication and lung damage through epigenetic imprinting","authors":["Wen Juan Tu","Michelle Melino","...","Sudha Rao"],"journal":"Nature Communications","date":"2023-06-27","pmid":"37369668","doi":"10.1038/s41467-023-39341-4"},{"title":"Ultrasensitive Detection of SARS‐CoV‑2 by Flexible Metal Oxide Field‐Effect Transistors","authors":["Sihui Hou","Mengge Wu","...","Xinge Yu"],"journal":"Advanced Functional Materials","date":"2023-06-19","pmid":"","doi":"10.1002/adfm.202301268"},{"title":"Two-Dimensional (2D) materials in the detection of SARS-CoV-2","authors":["Aytekin Uzunoglu","Evrim Gunes Altuntas","...","Ozum Ozoglu"],"journal":"Microchemical Journal","date":"2023-06-14","pmid":"","doi":"10.1016/j.microc.2023.108970"},{"title":"Genetically engineered coronavirus-specific effector cells for in situ synthesis of antiviral proteins","authors":["Parijat Bhatnagar","Marvin A. 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Lesteberg","Paula Araya","...","J. David Beckham"],"journal":"Frontiers in Immunology","date":"2023-02-02","pmid":"","doi":"10.3389/fimmu.2023.1113932"},{"title":"Spatial transcriptomic characterization of COVID-19 pneumonitis identifies immune circuits related to tissue injury.","authors":["Amy R Cross","Carlos E de Andrea","...","Fadi Issa"],"journal":"JCI insight","date":"2023-01-25","pmid":"36472908","doi":"10.1172/jci.insight.157837"},{"title":"Fluorophore-encapsulated nanobeads for on-site, rapid, and sensitive lateral flow assay","authors":["Sung Eun Seo","Eunsu Ryu","...","Oh Seok Kwon"],"journal":"Sensors and Actuators B: Chemical","date":"2023-01-13","pmid":"36684645","doi":"10.1016/j.snb.2023.133364"},{"title":"Guidelines for visualization and analysis of DC in tissues using multiparameter fluorescence microscopy imaging methods.","authors":["Felix Bayerl","David A Bejarano","...","Jan P Böttcher"],"journal":"European Journal of Immunology","date":"2023-01-09","pmid":"36623939","doi":"10.1002/eji.202249923"},{"title":"Replication and Injury Associated With SARS-CoV-2 in Cultured Hepatocytes","authors":["Suman Pradhan","Susan D. Rouster","...","Kenneth E. Sherman"],"journal":"Pathogens and Immunity","date":"2023-01-01","pmid":"","doi":"10.20411/pai.v8i2.648"},{"title":"Structural studies of functional and pathogenic amyloid fibrils","authors":["Lu, Jiahui "],"journal":"","date":"2023-01-01","pmid":"","doi":""},{"title":"Computational Microscopy of Glycoproteins: from Viruses to T Cells","authors":["Rosenfeld, Mia Aurora "],"journal":"","date":"2023-01-01","pmid":"","doi":""},{"title":"Neutralization sensitivity, fusogenicity, and infectivity of Omicron subvariants","authors":["Xue-Jun Wang","Lin Yao","...","Mai-Juan Ma"],"journal":"Genome Medicine","date":"2022-12-29","pmid":"","doi":"10.1186/s13073-022-01151-6"},{"title":"Bioinspired Plasmo-virus for Point-of-Care SARS-CoV-2 Detection","authors":["Younggeun Park","Byunghoon Ryu","...","Katsuo Kurabayashi"],"journal":"Nano Letters","date":"2022-12-27","pmid":"36573824","doi":"10.1021/acs.nanolett.2c03700"},{"title":"Control of SARS-CoV-2 infection by MT1-MMP-mediated shedding of ACE2","authors":["Xuanming Guo","Jianli Cao","...","Hoi Leong Xavier Wong"],"journal":"Nature Communications","date":"2022-12-23","pmid":"36564389","doi":"10.1038/s41467-022-35590-x"},{"title":"SARS-CoV-2 multi-variant rapid detector based on graphene transistor functionalized with an engineered dimeric ACE2 receptor","authors":["Alice Romagnoli","Mattia D’Agostino","...","Daniele Di Marino"],"journal":"Nano Today","date":"2022-12-15","pmid":"36536857","doi":"10.1016/j.nantod.2022.101729"},{"title":"Comparison of viral inactivation methods on the characteristics of extracellular vesicles from SARS‐CoV‐2 infected human lung epithelial cells","authors":["Supasek Kongsomros","Nutkridta Pongsakul","...","Somchai Chutipongtanate"],"journal":"Journal of Extracellular Vesicles","date":"2022-12-05","pmid":"36468940","doi":"10.1002/jev2.12291"},{"title":"COVID-19 can lead to rapid progression of cervical intraepithelial neoplasia by dysregulating the immune system: A Hypothesis","authors":["Sabeth Becker","Danny Jonigk","...","Meike Schild-Suhren"],"journal":"Journal of reproductive immunology","date":"2022-11-09","pmid":"","doi":"10.1016/j.jri.2022.103763"},{"title":"Calcium dobesilate reduces SARS-CoV-2 entry into endothelial cells by inhibiting virus binding to heparan sulfate.","authors":["Yulia Kiyan","Anna Schultalbers","...","Hermann Haller"],"journal":"Scientific Reports","date":"2022-10-11","pmid":"36207386","doi":""},{"title":"Identification and differential usage of a host metalloproteinase entry pathway by SARS-CoV-2 Delta and Omicron","authors":["Mehdi Benlarbi","Geneviève Laroche","...","Marceline Côté"],"journal":"iScience","date":"2022-10-10","pmid":"36254158","doi":""},{"title":"A novel antiviral formulation inhibits SARS-CoV-2 infection of human bronchial epithelium","authors":["Purves Kevin","Haverty Ruth","...","Fletcher Nicola F"],"journal":"bioRxiv","date":"2022-10-05","pmid":"","doi":"10.1101/2022.10.05.510928"},{"title":"Immunogenicity and protectivity of intranasally delivered vector-based heterologous prime-boost COVID-19 vaccine Sputnik V in mice and non-human primates.","authors":["Amir I Tukhvatulin","Ilya V Gordeychuk","...","Alexander L Gintsburg"],"journal":"Emerging microbes & infections","date":"2022-09-28","pmid":"36031930","doi":"10.1080/22221751.2022.2119169"},{"title":"Isolation of a human SARS-CoV-2 neutralizing antibody from a synthetic phage library and its conversion to fluorescent biosensors.","authors":["Haimei Li","Bo Zhu","...","Hiroshi Ueda"],"journal":"Scientific Reports","date":"2022-09-19","pmid":"36109569","doi":""},{"title":"Trans-synaptic dwelling of SARS-CoV-2 particles perturbs neural synapse organization and function","authors":["Partiot Emma","Hirschler Aurélie","...","Gaudin Raphael"],"journal":"bioRxiv","date":"2022-09-14","pmid":"","doi":"10.1101/2022.09.13.507484"},{"title":"Molecular Analyses of Clinical Isolates and Recombinant SARS-CoV-2 Carrying B.1 and B.1.617.2 Spike Mutations Suggest a Potential Role of Non-Spike Mutations in Infection Kinetics","authors":["Andrei Veleanu","Maximilian A. Kelch","...","Luiz Carlos Junior Alcantara"],"journal":"Viruses","date":"2022-09-12","pmid":"36146823","doi":""},{"title":"A Recombinant VSV-Based Bivalent Vaccine Effectively Protects against Both SARS-CoV-2 and Influenza A Virus Infection","authors":["Zhujun Ao","Maggie J. Ouyang","...","Tom Gallagher"],"journal":"Journal of virology","date":"2022-09-07","pmid":"36069551","doi":"10.1128/jvi.01337-22"},{"title":"Carbohydrate-binding protein from stinging nettle as fusion inhibitor for SARS-CoV-2 variants of concern","authors":["Emiel Vanhulle","Thomas D’huys","...","Kurt Vermeire"],"journal":"Frontiers in cellular and infection microbiology","date":"2022-08-30","pmid":"36111239","doi":"10.3389/fcimb.2022.989534"}]

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