SARS-CoV-2 Reagents and Services Related Citations

The COVID-19 pandemic, caused by SARS-CoV-2 virus, has resulted in unprecedented crisis to the global health. The SARS-CoV-2 has spread into over 188 countries and sickened over 10M people worldwide. A timely response to virus outbreaks in terms of the developments of both diagnostic tools and therapeutics is essential to combat such invisible enemies. To support these studies, Sino Biological has developed a comprehensive panel of antibodies and antigens for SARS-CoV-2. Sino Biological also specializes in recombinant antigen and antibody production. The ProVirTM collection is the world largest viral antigen bank, including over 800 proteins from 350 viral strains.

Up to 15th September, there are 200 publications that have cited SARS-CoV-2 reagents or services providing by Sino Biological Inc.

1.Renhong Yan, et al.Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2.Science.2020

2. Lamers, MM, et al.SARS-CoV-2 productively infects human gut enterocytes.Science.2020

3. Rockx, B, et al.Comparative pathogenesis of COVID-19, MERS, and SARS in a nonhuman primate model.Science.2020

4. Yu, J, et al.DNA vaccine protection against SARS-CoV-2 in rhesus macaques.Science.2020

5. Xiangyang Chi, et al.A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2.Science.2020

6. Zhe Lv, et al.Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent theraprutic antibody.Science.2020

7. Bin Ju, et al.Human neutralizing antibodies elicited by SARS-CoV-2 infection.Nature.2020

8. Linlin Bao, et al.The Pathogenicity of SARS-CoV-2 in hACE2 Transgenic Mice.Nature.2020

9. Dora Pinto, et al.Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody.Nature.2020

10. Bojkova, D, et al.Proteomics of SARS-CoV-2-infected host cells reveals therapy targets.Nature.2020

11. Liu, L, et al.Potent neutralizing antibodies directed to multiple epitopes on SARS-CoV-2 spike.Nature.2020

12. Ke, Z, et al.Structures and distributions of SARS-CoV-2 spike proteins on intact virions.Nature.2020

13. Cao, Y, et al.Potent neutralizing antibodies against SARS-CoV-2 identified by high-throughput single-cell sequencing of convalescent patients\' B cells.Cell.2020

14. Wrapp, Daniel, et al.Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies.Cell.2020

15. Sun, J, et al.Generation of a Broadly Useful Model for COVID-19 Pathogenesis, Vaccination, and Treatment.Cell.2020

16. Wang, H, et al.Development of an Inactivated Vaccine Candidate, BBIBP-CorV, with Potent Protection against SARS-CoV-2.Cell.2020

17. Dai, L, et al.A universal design of betacoronavirus vaccines against COVID-19, MERS and SARS.Cell.2020

18. Li, Q, et al.The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity.Cell.2020

19. Zhang, N, et al.A thermostable mRNA vaccine against COVID-19.Cell.2020

20. Simon, D, et al.Patients with immune-mediated inflammatory diseases receiving cytokine inhibitors have low prevalence of SARS-CoV-2 seroconversion.Nature Communications .2020

21. Jiang, HW, et al.SARS-CoV-2 proteome microarray for global profiling of COVID-19 specific IgG and IgM responses.Nature Communications .2020

22. Wang, C, et al.A human monoclonal antibody blocking SARS-CoV-2 infection.Nature Communications .2020

23. Ou, X, et al.Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV.Nature Communications .2020

24. Deng, W, et al.Ocular conjunctival inoculation of SARS-CoV-2 can cause mild COVID-19 in Rhesus macaques.Nature Communications .2020

25. Smith, TRF, et al.Immunogenicity of a DNA vaccine candidate for COVID-19.Nature Communications .2020

26. Noy-Porat, T, et al.A panel of human neutralizing mAbs targeting SARS-CoV-2 spike at multiple epitopes.Nature Communications .2020

27. Zhao, H, et al.A broad-spectrum virus- and host-targeting peptide against respiratory viruses including influenza virus and SARS-CoV-2.Nature Communications .2020

28. Feng, L, et al.An adenovirus-vectored COVID-19 vaccine confers protection from SARS-COV-2 challenge in rhesus macaques.Nature Communications .2020

29. Ni, L, et al.Detection of SARS-CoV-2-specific humoral and cellular immunity in COVID-19 convalescent individuals.Immunity.2020

30. Laczkó, D, et al.A single immunization with nucleoside-modified mRNA vaccines elicits strong cellular and humoral immune responses against SARS-CoV-2 in mice.Immunity.2020

31. Long, QX, et al.Antibody responses to SARS-CoV-2 in patients with COVID-19.Nature Medicine.2020

32. Amanat F, et al.A serological assay to detect SARS-CoV-2 seroconversion in humans.Nature Medicine.2020

33. McCallum, M, et al.Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation.Nat. Struct. Mol. Biol..2020

34. Wu, Y, et al.Identification of Human Single-Domain Antibodies against SARS-CoV-2.Cell Host Microbe.2020

35. Dieterle, M, et al.A replication-competent vesicular stomatitis virus for studies of SARS-CoV-2 spike-mediated cell entry and its inhibition.Cell Host & Microbe.2020

36. Stanifer, ML, et al.Critical Role of Type III Interferon in Controlling SARS-CoV-2 Infection in Human Intestinal Epithelial Cells.Cell Rep.2020

37. Zhang, H, et al.Activation of Peroxiredoxin 1 by Fluvastatin Effectively Protects from Inflammation and SARS-CoV-2.Cell Metabolism.2020

38. Huibin LvCross-reactive antibody response between SARS-CoV-2 and SARS-CoV infections.Cell Reports.2020

39. Yi, C, et al.Key residues of the receptor binding motif in the spike protein of SARS-CoV-2 that interact with ACE2 and neutralizing antibodies.Cell. Mol. Immunol..2020

40. Xiao, F, et al.Evidence for gastrointestinal infection of SARS-CoV-2.Gastroenterology.2020

41. Seo, G, et al.Rapid Detection of COVID-19 Causative Virus (SARS-CoV-2) in Human Nasopharyngeal Swab Specimens Using Field-Effect Transistor-Based Biosensor.ACS Nano.2020

42. Su, H, et al.Renal histopathological analysis of 26 postmortem findings of patients with COVID-19 in China.Kidney Int.2020

43. Ye, L, et al.Human monoclonal antibodies block the binding of SARS-CoV-2 spike protein to angiotensin converting enzyme 2 receptor.Cellular & Molecular Immunology.2020

44. Bing ZhaoRecapitulation of SARS-CoV-2 Infection and Cholangiocyte Damage with Human Liver Organoids.Protein&Cell.2020

45. Chia, WN, et al.Serological differentiation between COVID-19 and SARS infections.Emerg Microbes Infect.2020

46. Sun B, et al.Kinetics of SARS-CoV-2 specific IgM and IgG responses in COVID-19 patients.Emerg Microbes Infect.2020

47. Shan-Meng Lin, et al.Structure-Based Stabilization of Non-native Protein-Protein Interactions of Coronavirus Nucleocapsid Proteins in Antiviral Drug Design.J. Med. Chem..2020

48. Liu, X, et al.Therapeutic effects of dipyridamole on COVID-19 patients with coagulation dysfunction.Acta Pharm Sin B.2020

49. Liu, X, et al.Potential therapeutic effects of dipyridamole in the severely ill patients with COVID-19.Acta Pharm Sin B.2020

50. Okba, NMA, et al.Severe Acute Respiratory Syndrome Coronavirus 2-Specific Antibody Responses in Coronavirus Disease 2019 Patients.Emerging Infect. Dis..2020

51. Sangeun Jeon, et al.Identification of antiviral drug candidates against SARS-CoV-2 from FDA-approved drugs.Antimicrob Agents Chemother.2020

52. Zeng, W, et al.Biochemical characterization of SARS-CoV-2 nucleocapsid protein.Biochemical and Biophysical Research Communications.2020

53. Fujita, R, et al.Efficient production of recombinant SARS-CoV-2 spike protein using the baculovirus-silkworm system.Biochemical and Biophysical Research Communications.2020

54. Chen, Z, et al.A DNA Aptamer Based Method for Detection of SARS-CoV-2 Nucleocapsid Protein.Virol Sin.2020

55. Huang, S, et al.Assessing the application of a pseudovirus system for emerging SARS-CoV-2 and re-emerging avian influenza virus H5 subtypes in vaccine development.Biomedical Journal.2020

56. Musarrat, F, et al.The anti-HIV Drug Nelfinavir Mesylate (Viracept) is a Potent Inhibitor of Cell Fusion Caused by the SARSCoV-2 Spike (S) Glycoprotein Warranting further Evaluation as an Antiviral against COVID-19 infections.J Med Virol.2020

57. Pu, T, et al.Evaluate Severe Acute Respiratory Syndrome Coronavirus 2 Infectivity by Pseudoviral Particles.J. Med. Virol..2020

58. Carnevale, S, et al.Direct endothelial damage and vasculitis due to SARS-CoV-2 in small bowel submucosa of CoViD-19 patient with diarrhea.J. Med. Virol..2020

59. Prasad, ASV;Local Immunity Concept in the Context of the Novel Corona Viral Infection: A Consideration.BioRxiv.2020

60. Zeng, X, et al.Isolation of a human monoclonal antibody specific for the receptor binding domain of SARS-CoV-2 using a competitive phage biopanning strategy.Antibody Therapeutics.2020

61. Khan, S, et al.Analysis of Serologic Cross-Reactivity Between Common Human Coronaviruses and SARS-CoV-2 Using Coronavirus Antigen Microarray.BioRxiv.2020

62. Thornburg, N, et al.Isolation and characterization of SARS-CoV-2 from the first US COVID-19 patient.BioRxiv.2020

63. Chunyun Sun, et al.SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development.BioRxiv.2020

64. Milewska, A, et al.HTCC as a highly effective polymeric inhibitor of SARS-CoV-2 and MERS-CoV.BioRxiv.2020

65. Wang, C, et al.Lectin-like Intestinal Defensin Inhibits 2019-nCoV Spike binding to ACE2.BioRxiv.2020

66. Li, Y, et al.Potential host range of multiple SARS-like coronaviruses and an improved ACE2-Fc variant that is potent against both SARS-CoV-2 and SARS-CoV-1.BioRxiv.2020

67. Xiong, H, et al.Robust neutralization assay based on SARS-CoV-2 S-bearing vesicular stomatitis virus (VSV) pseudovirus and ACE2-overexpressed BHK21 cells.BioRxiv.2020

68. Zhang, Q, et al.SARS-CoV-2 neutralizing serum antibodies in cats: a serological investigation.BioRxiv.2020

69. Zhang, Y, et al.Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins using High-Resolution Mass Spectrometry.BioRxiv.2020

70. Liu, Y, et al.Functional and Genetic Analysis of Viral Receptor ACE2 Orthologs Reveals Broad Potential Host Range of SARS-CoV-2.BioRxiv.2020

71. Tan, X, et al.Rapid and quantitative detection of COVID-19 markers in micro-liter sized samples.BioRxiv.2020

72. Zhu, Y, et al.Cross-reactive neutralization of SARS-CoV-2 by serum antibodies from recovered SARS patients and immunized animals.BioRxiv.2020

73. Walter, JD, et al.Synthetic nanobodies targeting the SARS-CoV-2 receptor-binding domain.BioRxiv.2020

74. De Assis, RR, et al.Analysis of SARS-CoV-2 Antibodies in COVID-19 Convalescent Plasma using a Coronavirus Antigen Microarray.BioRxiv.2020

75. Chi X, et al.Humanized Single Domain Antibodies Neutralize SARS-CoV-2 by Targeting Spike Receptor Binding Domain.BioRxiv.2020

76. Kim, SY, et al.Glycosaminoglycan binding motif at S1/S2 proteolytic cleavage site on spike glycoprotein may facilitate novel coronavirus (SARS-CoV-2) host cell entry.BioRxiv.2020

77. Si L, et al.Human organs-on-chips as tools for repurposing approved drugs as potential influenza and COVID19 therapeutics in viral pandemics.BioRxiv.2020

78. Liu L, et al.SARS-CoV-2 spike protein binds heparan sulfate in a length-and sequence-dependent manner.BioRxiv.2020

79. Zha L, et al.Development of a COVID-19 vaccine based on the receptor binding domain displayed on virus-like particles.BioRxiv.2020

80. Romano, M, et al.An engineered stable mini-protein to plug SARS-Cov2 Spikes.BioRxiv.2020

81. Liu, Y, et al.Functional and Genetic Analysis of Viral Receptor ACE2 Orthologs Reveals a Broad Potential Host Range of SARS-CoV-2.BioRxiv.2020

82. De Assis, RR, et al.Analysis of SARS-CoV-2 Antibodies in COVID-19 Convalescent Blood using a Coronavirus Antigen Microarray.BioRxiv.2020

83. Hedde, PN, et al.A Modular Microarray Imaging System for Highly Specific COVID-19 Antibody Testing.BioRxiv.2020

84. Ghazizadeh, Z, et al.Androgen regulates SARS-CoV-2 receptor levels and is associated with severe COVID-19 symptoms in men.BioRxiv.2020

85. Finch, CL, et al.Characteristic and quantifiable COVID-19-like abnormalities in CT-and PET/CT-imaged lungs of SARS-CoV-2-infected crab-eating macaques (Macaca fascicularis).BioRxiv.2020

86. Cai, Y, et al.Distinct conformational states of SARS-CoV-2 spike protein.BioRxiv.2020

87. Zang, J, et al.Immunization with the receptor–binding domain of SARS-CoV-2 elicits antibodies cross-neutralizing SARS-CoV-2 and SARS-CoV without antibody-dependent enhancement.BioRxiv.2020

88. Zost, SJ, et al.Rapid isolation and profiling of a diverse panel of human monoclonal antibodies targeting the SARS-CoV-2 spike protein.BioRxiv.2020

89. Zhang, Y, et al.The ORF8 Protein of SARS-CoV-2 Mediates Immune Evasion through Potently Downregulating MHC-I.BioRxiv.2020

90. Corbett, K, et al.SARS-CoV-2 mRNA Vaccine Development Enabled by Prototype Pathogen Preparedness.BioRxiv.2020

91. Yang, Y, et al.The utility of native MS for understanding the mechanism of action of repurposed therapeutics in COVID-19: heparin as a disruptor of the SARS-CoV-2 interaction with its host cell receptor.BioRxiv.2020

92. Daly, J, et al.Neuropilin-1 is a host factor for SARS-CoV-2 infection.BioRxiv.2020

93. Liu, D, et al.Ultra-sensitive nanozyme-based chemiluminescence paper test for rapid diagnosis of SARS-CoV-2 infection.BioRxiv.2020

94. Mesci, P, et al.Sofosbuvir protects human brain organoids against SARS-CoV-2.BioRxiv.2020

95. Bosco-Lauth, A, et al.Pathogenesis, transmission and response to re-exposure of SARS-CoV-2 in domestic cats.BioRxiv.2020

96. Yao, D, et al.Human H-ferritin presenting RBM of spike glycoprotein as potential vaccine of SARS-CoV-2.BioRxiv.2020

97. Liu, L, et al.A translatable subunit nanovaccine for COVID-19.Chem Rxiv.2020

98. Song, Y, et al.Discovery of Aptamers Targeting Receptor-Binding Domain of the SARS-CoV-2 Spike Glycoprotein.ChemRxiv.2020

99. Sobrevilla, JMV;¿ Por qué los pacientes con diabetes o hipertensión son más susceptibles a tener COVID-19?.Conference.2020

100. Harcourt, Jennifer, et al.Severe Acute Respiratory Syndrome Coronavirus 2 from Patient with Coronavirus Disease, United States.Emerging Infectious Diseases.2020

101. Feng, Siqin, et al.Eltrombopag is a potential target for drug intervention in SARS-CoV-2 spike protein.Infection, Genetics and Evolution : Journal of Molecular Epidemiology and Evolutionary Genetics in Infectious Diseases.2020

102. Zeng, X, et al.Molecular Detection of SARS-CoV-2 in Formalin Fixed Paraffin Embedded Specimens.JCI Insight.2020

103. Larsen, CP, et al.Collapsing Glomerulopathy in a Patient With Coronavirus Disease 2019 (COVID-19).Kidney Int Rep.2020

104. Jiang, H, et al.Global profiling of SARS-CoV-2 specific IgG/IgM responses of convalescents using a proteome microarray.medRxiv.2020

105. Bo Diao, et al.Human Kidney is a Target for Novel Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Infection.medRxiv.2020

106. Linlin Bao, et al.Reinfection could not occur in SARS-CoV-2 infected rhesus macaques.medRxiv.2020

107. Linlin Bao, et al.Rhesus macaques can be effectively infected with SARS-CoV-2 via ocular conjunctival route.medRxiv.2020

108. Ke Wang, et al.SARS-CoV-2 invades host cells via a novel route: CD147-spike protein.medRxiv.2020

109. Feng, Z, et al.The Novel Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Directly Decimates Human Spleens and Lymph Nodes.medRxiv.2020

110. Wei, C, et al.Cholesterol Metabolism--Impact for SARS-CoV-2 Infection Prognosis, Entry, and Antiviral Therapies.medRxiv.2020

111. McAndrews, KM, et al.Identification of IgG antibody response to SARS-CoV-2 spike protein and its receptor binding domain does not predict rapid recovery from COVID-19.medRxiv.2020

112. Norman, M, et al.Ultra-Sensitive High-Resolution Profiling of Anti-SARS-CoV-2 Antibodies for Detecting Early Seroconversion in COVID-19 Patients.medRxiv.2020

113. Randad, PR, et al.COVID-19 serology at population scale: SARS-CoV-2-specific antibody responses in saliva.medRxiv.2020

114. Rosenberg, ES, et al.Cumulative incidence and diagnosis of SARS-CoV-2 infection in New York.medRxiv.2020

115. Phipps, WS, et al.SARS-CoV-2 Antibody responses do not predict COVID-19 disease severity.medRxiv.2020

116. Chakraborty, S, et al.Symptomatic SARS-CoV-2 infections display specific IgG Fc structures.medRxiv.2020

117. Rosendal, E, et al.Detection of asymptomatic SARS-CoV-2 exposed individuals by a sensitive S-based ELISA..medRxiv.2020

118. Mittal, A, et al.COVID-19 Pandemic: Insights into Structure, Function, and hACE2 Receptor Recognition by the SARS-CoV-2.preprints.2020

119. Simon, D, et al.Patients with immune-mediated inflammatory diseases receiving cytokine inhibitors have low prevalence of SARS-CoV-2 infection.Research Square.2020

120. Kanjanasirirat, P, et al.High-Content Screening of Thai Medicinal Plants Reveals Boesenbergia rotunda Extract and its Component Panduratin A as Anti-SARS-CoV-2 Agents.Research Square.2020

121. Yang, J, et al.Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor.Research Square.2020

122. Bdr-Eldeen, O;What we should understand about SARS-COV-2

123. Ravichandran, Supriya, et al.Antibody signature induced by SARS-CoV-2 spike protein immunogens in rabbits.Science Translational Medicine.2020

124. Zhou, R, et al.Acute SARS-CoV-2 Infection Impairs Dendritic Cell and T Cell Responses.SSRN Journal.2020

125. Cheng, Y, et al.Furin Inhibitors Block SARS-CoV-2 Spike Protein Cleavage to Suppress Virus Production and Cytopathic Effects.SSRN Journal.2020

126. 彭浩然, et al.上海 2 株严重急性呼吸综合征冠状病毒 2 的分离与鉴定.第二军医大学学报.2020

127. Yu, P, et al.Age-related rhesus macaque models of COVID-19.Anim Models Exp Med.2020

128. Turista, D, et al.Distribution of COVID-19 and Phylogenetic Tree Construction of SARS-CoV-2 in Indonesia.J. Pure Appl. Microbiol..2020

129. Belete, T;A review on Promising vaccine development progress for COVID-19 disease.Vacunas.2020

130. Gan, JH;Discovery of small molecule therapeutics for the Middle Eastern respiratory syndrome-coronavirus (MERS-CoV).Thesis.2020

131. Wang, C, et al.Alveolar macrophage dysfunction and cytokine storm in the pathogenesis of two severe COVID-19 patients.EBioMedicine.2020

132. Lei, H, et al.SARS-CoV-2 environmental contamination associated with persistently infected COVID-19 patients.Influenza Other Respir Viruses.2020

133. Liu, L, et al.Potent Neutralizing Monoclonal Antibodies Directed to Multiple Epitopes on the SARS-CoV-2 Spike.BioRxiv.2020

134. Beddingfield, B;Iwanaga, N, et al.The Integrin Binding Peptide, ATN-161, as a Novel Therapy for SARS-CoV-2 Infection.BioRxiv.2020

135. Salazar, E, et al.Relationship between Anti-Spike Protein Antibody Titers and SARS-CoV-2 In Vitro Virus Neutralization in Convalescent Plasma.BioRxiv.2020

136. Hanson, QM, et al.Targeting ACE2-RBD interaction as a platform for COVID19 therapeutics: Development and drug repurposing screen of an AlphaLISA proximity assay.BioRxiv.2020

137. Giobbe, G, et al.SARS-CoV-2 infection and replication in human fetal and pediatric gastric organoids.BioRxiv.2020

138. Wang, N, et al.Chloroquine and hydroxychloroquine as ACE2 blockers to inhibit viropexis of COVID-19 Spike pseudotype virus.BioRxiv.2020

139. Liu, J, et al.Engineered human mesenchymal stem cells as new vaccine platform for COVID-19.BioRxiv.2020

140. Hu, J, et al.The D614G mutation of SARS-CoV-2 spike protein enhances viral infectivity and decreases neutralization sensitivity to individual convalescent sera.BioRxiv.2020

141. Klimstra, W, et al.SARS-CoV-2 growth, furin-cleavage-site adaptation and neutralization using serum from acutely infected, hospitalized COVID-19 patients.BioRxiv.2020

142. den Hartog, G, et al.SARS-CoV-2-specific antibody detection for sero-epidemiology: a multiplex analysis approach accounting for accurate seroprevalence.medRxiv.2020

143. Yahalom-Ronen, Y, et al.A single dose of recombinant VSV-ΔG-spike vaccine provides protection against SARS-CoV-2 challenge.BioRxiv.2020

144. Mulgaonkar, N, et al.Bcr-Abl tyrosine kinase inhibitor imatinib as a potential drug for COVID-19.BioRxiv.2020

145. Blair, R;Vaccari, M, et al.ARDS and Cytokine Storm in SARS-CoV-2 Infected Caribbean Vervets.BioRxiv.2020

146. Walker, S, et al.SARS-CoV-2 assays to detect functional antibody responses that block ACE2 recognition in vaccinated animals and infected patients.BioRxiv.2020

147. Stukalov, A, et al.Multi-level proteomics reveals host-perturbation strategies of SARS-CoV-2 and SARS-CoV.BioRxiv.2020

148. Liu, T, et al.High-Accuracy Multiplexed SARS-CoV-2 Antibody Assay with Avidity and Saliva Capability on a Nano-Plasmonic Platform.BioRxiv.2020

149. Steiner, D, et al.Array-based analysis of SARS-CoV-2, other coronaviruses, and influenza antibodies in convalescent COVID-19 patients.BioRxiv.2020

150. Ozono, S, et al.Naturally mutated spike proteins of SARS-CoV-2 variants show differential levels of cell entry.BioRxiv.2020

151. Zhang, J, et al.Cross-reactivity of neutralizing antibody and its correlation with circulating T follicular cells in recovered COVID-19 individuals.medRxiv.2020

152. Zhou, D, et al.Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient.BioRxiv.2020

153. Zang, R, et al.Cholesterol 25-hydroxylase suppresses SARS-CoV-2 replication by blocking membrane fusion.BioRxiv.2020

154. Zhang, G, et al.Investigation of ACE2 N-terminal fragments binding to SARS-CoV-2 Spike RBD.BioRxiv.2020

155. Hernandez, J, et al.Dodging COVID-19 infection: Low expression and localization of Angiotensin-Converting Enzyme 2 (ACE2) and Transmembrane Serine Protease 2 (TMPRSS2) in Mesenchymal Stem Cells derived from human umbilical cord (hUC-MSCs)..Research Square.2020

156. Wu, S, et al.A single dose of an adenovirus-vectored vaccine provides complete protection of the upper and lower respiratory tracts against SARS-CoV-2 challenge.Research Square.2020

157. Liu, L;Clinical and pathological findings of SARS-CoV-2 infection and concurrent IgA nephropathy: A case report.Research Square.2020

158. Ren, L, et al.The Kinetics of Humoral Response and its Relationship with the Disease Severity in COVID-19.Research Square.2020

159. Tang, X, et al.Spike protein up-regulates inflammatory axis of both thromboinflammation and leukotriene in severe COVID-19.Research Square.2020

160. Zhang, X, et al.Engineering mesenchymal stem cells with neutralizing and anti- inflammation dual-capability against SARS-CoV-2 infection.Research Square.2020

161. Ahmadivand, A, et al.Femtomolar-level detection of SARS-CoV-2 spike proteins using toroidal plasmonic metasensors.arXiv preprint.2020

162. Baker, AN, et al.The SARS-COV-2 spike protein binds sialic acids, and enables rapid detection in a lateral flow point of care diagnostic device.PrePrint.2020

163. 彭浩然, et al.严重急性呼吸综合征冠状病毒 2 假病毒的制备及验证.第二军医大学 .2020

164. Ratajczak, MZ, et al.SARS-CoV-2 Entry Receptor ACE2 Is Expressed on Very Small CD45- Precursors of Hematopoietic and Endothelial Cells and in Response to Virus Spike Protein Activates the Nlrp3 Inflammasome.Stem Cell Rev Rep.2020

165. Hu, J, et al.Development of cell-based pseudovirus entry assay to identify potential viral entry inhibitors and neutralizing antibodies against SARS-CoV-2.Genes & Diseases.2020

166. Xu, L, et al.COVID-19-like symptoms observed in Chinese tree shrews infected with SARS-CoV-2.Zool Res.2020

167. Wang, Y, et al.SARS-CoV-2 S1 is superior to the RBD as a COVID-19 subunit vaccine antigen.J. Med. Virol..2020

168. Chiuppesi, F, et al.Development of a Multi-Antigenic SARS-CoV-2 Vaccine Using a Synthetic Poxvirus Platform.Res Sq.2020

169. Kumar, D, et al.Prospective Observational Study of Screening Asymptomatic Healthcare Workers for SARS-CoV-2 at a Canadian Tertiary Care Center.medRxiv.2020

170. Cate, D, et al.Antibody Screening Results for Anti-Nucleocapsid Antibodies Towards the Development of a SARS-CoV-2 Nucleocapsid Protein Antigen Detecting Lateral Flow Assay.ChemRxiv.2020

171. Feng, Z, et al.Detection of the SARS-CoV-2 Nucleocaspid Protein (NP) Using Immunohistochemistry.BIO-PROTOCOL.2020

172. Li, Q, et al.The Impact of Natural and Glycosylation Mutations in the SARS-CoV-2 Spike Protein on Viral Infectivity and Antigenicity.SSRN Journal.

173. Tosif, S, et al.Immune responses to SARS-CoV-2 in children of parents with symptomatic COVID-19.Research Square. 2020

174. Brocato, RL, et al.Disruption of Adaptive Immunity Enhances Disease in SARS-CoV-2 Infected Syrian Hamsters.Research Square. 2020

175. Gorshkov, K, et al.Quantum Dot-Conjugated SARS-CoV-2 Spike Pseudo-Virions Enable Tracking of Angiotensin Converting Enzyme 2 Binding and Endocytosis.ACS Nano. 2020

176. Tan, X, et al.Rapid and quantitative detection of SARS-CoV-2 specific IgG for convalescent serum evaluation.Biosensors and Bioelectronics. 2020

177. Al-Dalahmah, O, et al.Neuronophagia and microglial nodules in a SARS-CoV-2 patient with cerebellar hemorrhage.Acta Neuropathol Commun. 2020

178. McAndrews, KM, et al.Heterogeneous antibodies against SARS-CoV-2 spike receptor binding domain and nucleocapsid with implications on COVID-19 immunity.JCI Insight.2020

179. van Tol, S, et al.Accurate Serology for SARS-CoV-2 and common Human Coronaviruses using a Multiplex Approach.Emerg Microbes Infect. 2020

180. Li, Y, et al.SARS-CoV-2 and three related coronaviruses utilize multiple ACE2 orthologs and are potently blocked by an improved ACE2-Ig.J. Virol.. 2020

181. Wang, N, et al.Chloroquine and hydroxychloroquine as ACE2 blockers to inhibit viropexis of 2019-nCoV Spike pseudotyped virus.Phytomedicine. 2020

182. Saha, R, et al.Repurposing Drugs, Ongoing Vaccine, and New Therapeutic Development Initiatives Against COVID-19.Front. Pharmacol.. 2020

183. Mirzaei, R, et al.Overview of the current promising approaches for the development of an effective severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) vaccine.Int. Immunopharmacol.. 2020

184. Xiao, C, et al.Human post-infection serological response to the spike and nucleocapsid proteins of SARS-CoV-2.Influenza Other Respir Viruses. 2020

185. Wheeler, SE, et al.Evaluation of SARS-CoV-2 prototype serologic test in hospitalized patients.Clin. Biochem.. 2020

186. Li, N, et al.Molecular diagnosis of COVID‑19: Current situation and trend in China (Review).Exp Ther Med. 2020

187. Yang, R, et al.Development and effectiveness of Pseudotyped SARS-CoV-2 system as determined by neutralizing efficiency and entry inhibition test in vitro.Biosaf Health. 2020

188. Liu, L, et al.Subunit Nanovaccine with Potent Cellular and Mucosal Immunity for COVID-19.ACS Appl. Bio Mater.. 2020

189. Wang, G, et al.Degradation of SARS-CoV-2 Receptor ACE2 by Tobacco Carcinogens.SSRN Journal. 2020

190. Liu, Z, et al.The recombinant subunit vaccine RBD-Fc, consisting of SARS-CoV-2 RBD and human IgG Fc as an immunopotentiator, elicits robust neutralizing antibody responses against SARS-CoV-2 infection.Research Square. 2020

191. Azad, T, et al.Nanoluciferase complementation-based biosensor reveals the importance of N- linked glycosylation of SARS-CoV-2 Spike for viral entry.Research Square. 2020

192. Grant, BD, et al.A SARS-CoV-2 Coronavirus Nucleocapsid Protein Antigen-Detecting Lateral Flow Assay.ChemRxiv. 2020

193. Renn, A, et al.Fruitful neutralizing antibody pipeline brings hope to defeat SARS-Cov-2.Trends in Pharmacological Sciences. 2020

194. Ko, M, et al.Comparative analysis of antiviral efficacy of FDA-approved drugs against SARS-CoV-2 in human lung cells.J. Med. Virol.. 2020

195. Hsu, A, et al.Placental SARS-CoV-2 in a Pregnant Woman with Mild COVID-19 Disease.J. Med. Virol.. 2020

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Here we list part products cited in those publications.

Cat# Molecule Description Total Cites Citation Number
40591-V08H Spike S1 SARS-CoV-2 Spike S1 Protein, His tag, HPLC-verified 22 8, 24, 25, 34, 41, 43, 46, 61, 63, 65, 69, 71, 74, 82, 106, 107, 110, 112, 123, 127, 142, 148
40589-V08B1 Spike S1+S2 ECD SARS-CoV-2 Spike S1+S2 ECD Protein, His tag 19 13, 25, 61, 69, 73, 74, 75, 78, 82, 98, 110, 113, 123, 132, 139, 146, 149, 152, 156
40592-V05H Spike RBD SARS-CoV-2 Spike RBD Protein, mFc tag, HPLC-verified 13 1, 9, 14, 43, 61, 67, 73, 74, 75, 82, 87, 88, 98
40150-V08B1 Spike S1 SARS-CoV Spike S1 Protein, His tag 11 9, 25, 31, 61, 63, 72, 74, 75, 82, 136, 151
40592-V08B Spike RBD SARS-CoV-2 Spike RBD Protein, His tag 9 13, 34, 43, 60, 75, 98, 142, 149, 154
40588-V08B NP-CoV SARS-CoV-2 NP-CoV Protein, His tag 8 46, 61, 74, 82, 113, 115, 132, 142
40590-V08B Spike S2 SARS-CoV-2 Spike S2 Protein, His tag 8 38, 61, 72, 74, 82, 123, 149, 151
40143-V08B NP-CoV SARS-CoV NP-CoV Protein, His tag 6 31, 50, 61, 74, 82, 35
40591-V02H Spike S1 SARS-CoV-2 Spike S1 Protein, Fc tag 6 61, 70, 74, 81, 82, 131
40592-V08H Spike RBD SARS-CoV-2 Spike RBD Protein, His tag 6 80, 111, 113, 123, 144, 148
40069-V08H Spike S1 MERS-CoV Spike S1 Protein, His tag 5 41, 61, 63, 74, 82
40150-V08B2 Spike RBD SARS-CoV Spike RBD Protein, His tag 5 61, 72, 74, 82, 149
40605-V08B Spike S1+S2 ECD HCoV-229E Spike S1+S2 ECD Protein, His tag 5 61, 74, 82, 113, 149
10108-H08H ACE2 Human ACE2 Protein, His tag, HPLC-verified 5 43, 75, 98, 17, 136
40069-V08B Spike S1+S2 ECD MERS-CoV Spike S1+S2 ECD Protein, His tag 5 61, 74, 82, 152, 159
40069-V08B1 Spike S1 MERS-CoV Spike S1 Protein, His tag 5 61, 74, 82, 149, 151
40607-V08B Spike S1+S2 ECD HCoV-OC43 Spike S1+S2 ECD Protein, His tag 5 61, 74, 82, 149, 152
40150-V31B2 Spike RBD SARS-CoV Spike RBD Protein, rFc Tag 4 61, 63, 74, 82
40600-V08H Spike S1 HCoV-NL63 Spike S1 Protein, His tag 4 32, 61, 74, 82
40601-V08H Spike S1 HCoV-229E Spike S1 Protein, His tag 4 32, 61, 74, 82
40070-V08B Spike S2 MERS-CoV Spike S2 Protein, His tag 4 61, 74, 82, 151
40071-V08B1 Spike RBD MERS-CoV Spike RBD Protein, His tag 4 61, 74, 82, 149
40606-V08B Spike S1+S2 ECD HCoV-HKU1 Spike S1+S2 ECD Protein, His tag 4 61, 74, 82, 149
10003-V06H1 HA1 H5N1 HA1 Protein, His & Fc Tag 3 61, 74, 82
10003-V06H3 HA1 H5N1 HA1 Protein, His & Fc Tag 3 61, 74, 82
11049-V08B RSV-F RSV RSV-F Protein, His tag 3 61, 74, 82
11070-V08H RSV-G RSV RSV-G Protein, His tag 3 61, 74, 82
11716-V08H HA1 Influenza B HA1 Protein, His tag 3 61, 74, 82
11716-V08H1 HA1 Influenza B HA1 Protein, His tag 3 61, 74, 82
13029-V08H RSV-G RSV RSV-G Protein, His tag 3 61, 74, 82
40021-V08H Spike S1 HCoV-HKU1 Spike S1 Protein, His tag 3 61, 74, 82
40035-V08H HA1 H1N1 HA1 Protein, His tag 3 61, 74, 82
40035-V08H1 HA1 H1N1 HA1 Protein, His tag 3 61, 74, 82
40037-V08B RSV-F RSV RSV-F Protein, His tag 3 61, 74, 82
40068-V08B NP-CoV MERS-CoV NP-CoV Protein, His tag 3 61, 74, 82
40071-V05B Spike RBD MERS-CoV Spike RBD Protein, mFc Tag 3 61, 74, 82
40071-V31B Spike RBD MERS-CoV Spike RBD Protein, rFc Tag 3 61, 74, 82
40071-V31B1 Spike RBD MERS-CoV Spike RBD Protein, rFc Tag 3 61, 74, 82
40103-V08H HA1 H7N9 HA1 Protein, His tag 3 61, 74, 82
40103-V08H1 HA1 H7N9 HA1 Protein, His tag 3 61, 74, 82
40354-V08B HA1 H3N2 HA1 Protein, His tag 3 61, 74, 82
40354-V08H1 HA1 H3N2 HA1 Protein, His tag 3 61, 74, 82
40458-V08B DcCoV-NP DcCoV DcCoV-NP Protein, His tag 3 61, 74, 82
40498-V08B HA Influenza B HA Protein, His tag 3 61, 74, 82
40498-V08H1 HA Influenza B HA Protein, His tag 3 61, 74, 82
40524-V08E PLpro SARS-CoV PLpro Protein, His tag 3 61, 74, 82
40591-V05H1 Spike S1 SARS-CoV-2 Spike S1 Protein, mFc Tag 3 61, 74, 82
40602-V08H Spike S1 HCoV-HKU1 Spike S1 Protein, His tag 3 61, 74, 82
40603-V08H HE-CoV HCoV-OC43 HE-CoV Protein, His tag 3 61, 74, 82
40604-V08B Spike S1+S2 ECD HCoV-NL63 Spike S1+S2 ECD Protein, His tag 3 61, 74, 82
10108-H02H ACE2 Human ACE2 Protein, Fc tag 3 65, 134, 140
40591-V08B1 Spike S1 SARS-CoV-2 Spike S1 Protein, His tag 3 110, 149, 151
10108-H05H ACE2 Human ACE2 Protein, Fc tag 2 60, 146
40592-V02H Spike RBD SARS-CoV-2 Spike RBD Protein, Fc tag 2 84, 136
40634-V08B Spike S1+S2 ECD SARS-CoV Spike S1+S2 ECD Protein, His tag 2 149, 152
10108-H08B ACE2 Human ACE2 Protein, His tag, HPLC-verified 1 13
10602-HNAE TNF Human TNF Protein, native 1 34
40592-V08B-B Spike RBD SARS-CoV-2 Spike RBD Protein, His tag 1 13
40592-V31H Spike RBD SARS-CoV-2 Spike RBD Protein, rFc Tag 1 9
10395-HNAE IL6 human IL6 Protein, 1 160
11055-V08B HA H1N1 HA Protein, His tag 1 149
11056-V08B HA H3N2 HA Protein, His tag 1 149
11692-V08B HA H1N1 HA Protein, His tag 1 149
Cat# Description Antigen Type Total Cites Citation Number
40150-R007 SARS-CoV-2 Spike Antibody Spike Rabbit MAb 5 41, 65, 108, 141, 157
40143-T62 SARS-CoV NP-CoV Antibody NP-CoV Rabbit PAb 4 3, 40, 42, 49
40150-T52 SARS-CoV Spike Antibody Spike Rabbit PAb 4 57, 62, 63, 100
40143-R019 SARS-CoV-2 NP-CoV Antibody NP-CoV Rabbit MAb 4 10, 103, 109, 141
40592-T62 SARS-CoV-2 Spike RBD Antibody Spike RBD Rabbit PAb 4 61, 74, 82, 153
40150-T62 SARS-CoV Spike S1 Antibody Spike S1 Rabbit PAb 3 23, 102, 118
40143-R001 SARS-CoV NP-CoV Antibody NP-CoV Rabbit MAb 3 51, 105, 135
10108-RP01 Human ACE2 Antibody ACE2 Rabbit PAb 2 44, 109
40143-MM05 SARS-CoV Nucleocapsid Antibody Nucleocapsid Mouse MAb 2 36, 137
10108-T56 Human ACE2 Antibody ACE2 Rabbit PAb 1 40
11695-RP01 HIV Gag-p24 Antibody Gag-p24 Rabbit PAb 1 23
11973-MM05T-H other M13 Antibody M13 Mouse MAb 1 60
40068-MM10 MERS-CoV NP-CoV Antibody NP-CoV Mouse MAb 1 64
40068-RP02 MERS-CoV NP-CoV Antibody NP-CoV Rabbit PAb 1 47
40070-MM11 MERS-CoV Spike s2 Antibody Spike s2 Mouse MAb 1 23
40150-D001 SARS-CoV Spike Antibody Spike Chimeric MAb 1 77
40150-MM02 SARS-CoV Spike S1 Antibody Spike S1 Mouse MAb 1 23
40150-RP01 SARS-CoV Spike S1 Antibody Spike S1 Rabbit PAb 1 63
HG1K Human IgG1, kappa Isotype Control     1 13
SSA009 Goat Anti-Human IgG Secondary Antibody (Biotin)     1 29
40590-T62 SARS-CoV-2 Spike S2 Antibody Spike S2 Rabbit PAb 1 153
Recombinant Antibody Production