Anti-SARS-CoV-2 Spike RBD (Clone: 2165)- Purified No Carrier Protein

Referencia LT1900-500

embalaje : 500ug

Marca : Leinco Technologies

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AntiSARSCoV2 Spike RBD [Clone 2165] — Purified No Carrier Protein

Product No.: LT1900

Product No.LT1900
Clone
2165
Target
SARSCoV2 RBD
Product Type
Recombinant Monoclonal Antibody
Alternate Names
SARSCoV2 Spike RBD Antibody, Receptor Binding Domain Antibody
Isotype
Human IgG1
Applications
ELISA
,
IHC
,
N

Data

AntiSARS CoV2 RBD, Clone 2165 ELISA DataCoating: Purified Recombinant SARSCoV2 Spike RBD (Prod. No. S851), concentration of 1 ug/ml, 100 ul/well overnight at 28°C. Detection: AntiSARSCoV2 RBD (Clone 2165) conjugated to HRP was serially diluted starting at 25 ng/ml down to 0.23 ng/ml, 100 ul/well for 1 hour at 37°C. Substrate: TMB (Leinco T118), 100 ul/well for 15 min. at room temperature followed by Leinco 450 nm Stop Solution (Leinco T125), 50 ul/well.
AntiSARSCoV2 RBD (Clone 2165) Neutralizing AntibodyLeinco’s AntiSARSCoV2 Antibody to the Receptor Binding Domain (RBD) (Clone 2165). Antibody binds to RBD and blocks binding to the ACE2 receptor on coated plates using Leinco’s patent pending COVID19 ImmunoRankTM Neutralization MICROELISA Assay (Prod. No. S2000).

Antibody Details

Product Details

Reactive Species
SARSCoV2
Virus
Expression Host
HEK293 Cells
Immunogen
Sequenced from human survivors of COVID19 (SARSCoV2)
Product Concentration
≥1.0 mg/ml
Purity
≥90% monomer by analytical SEC and SDSPage
Formulation
This recombinant monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.
Product Preparation
Recombinant antibodies are manufactured in an animal free facility using only in vitro protein free cell culture techniques and are purified by a multistep process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.
Storage and Handling
This antibody may be stored sterile as received at 28°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at ≤ 70°C. Avoid Repeated Freeze Thaw Cycles.
Country of Origin
USA
Shipping
Standard Overnight on Blue Ice.
Applications and Recommended Usage?
Quality Tested by Leinco
ELISA
Additional Applications Reported In Literature ?
N
IHC
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.

Description

Description

Specificity
AntiSARSCoV2 Spike RBD, clone 2165, specifically targets an epitope on the SARSCoV2 spike protein receptorbinding domain (RBD).
Background
Severe acute respiratory syndrome coronavirus 2 (SARSCoV2), the causative agent of coronavirus disease 2019 (COVID19), is an enveloped, singlestranded, positivesense RNA virus that belongs to the Coronaviridae family 1. The SARSCoV2 genome, which shares 79.6% identity with SARSCoV, encodes four essential structural proteins: the spike (S), envelope (E), membrane (M), and nucleocapsid protein (N) 2. The S protein is a transmembrane, homotrimeric, class I fusion glycoprotein that mediates viral attachment, fusion, and entry into host cells 3. Each ~180 kDa monomer contains two functional subunits, S1 (~700 a.a) and S2 (~600 a.a), that mediate viral attachment and membrane fusion, respectively. S1 contains two major domains, the Nterminal (NTD) and Cterminal domains (CTD). The CTD contains the receptorbinding domain (RBD), which binds to the angiotensinconverting enzyme 2 (ACE2) receptor on host cells 35. Although both SARSCoV and SARSCoV2 bind the ACE2 receptor, the RBDs only share ~73% amino acid identity, and the SARSCoV2 RBD binds with a higher affinity compared to SARSCoV 3, 6. The RBD is dynamic and undergoes hingelike conformational changes, referred to as the “down” or “up” conformations, which hide or expose the receptorbinding motifs, respectively 7. Following receptor binding, S1 destabilizes, and TMPRSS2 cleaves S2, which undergoes a pre to postfusion conformation transition, allowing for membrane fusion 8, 9.

Polyclonal RBDspecific antibodies can block ACE2 binding 10, 11, and antiRBD neutralizing antibodies are present in the sera of convalescent COVID19 patients 12, identifying the RBD as an attractive candidate for vaccines and therapeutics. In addition, the RBD is poorly conserved, making it a promising antigen for diagnostic tests 13 14. Serologic tests for the RBD are highly sensitive and specific for detecting SARSCoV2 antibodies in COVID19 patients 13 15. Furthermore, the levels of antiRBD antibodies correlated with SARSCoV2 neutralizing antibodies, suggesting the RBD could be used to predict an individual's risk of disease 13.
Antigen Distribution
The spike RBD is expressed on the surface of SARSCoV2.
Research Area
COVID19
.
Infectious Disease
.
Seasonal and Respiratory Infections
.
Viral
.
IVD Raw Material

References & Citations

1. Zhou, P., Yang, X., Wang, X. et al. Nature 579, 270–273. 2020.
2. Wu, F., Zhao, S., Yu, B. et al. Nature 579, 265–269. 2020.
3. Wrapp D, Wang N, Corbett KS, et al. bioRxiv. 2020.02.11.944462. 2020.
4. Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Cell. 181(2):281292.e6. 2020.
5. Li W, Zhang C, Sui J, et al. EMBO J. 24(8):16341643. 2005.
6. Shang, J., Ye, G., Shi, K. et al. Nature 581, 221–224. 2020.
7. Gui M, Song W, Zhou H, et al. Cell Res. 27(1):119129. 2017.
8. Walls AC, Tortorici MA, Snijder J, et al. Proc Natl Acad Sci U S A. 114(42):1115711162. 2017.
9. Hoffmann M, KleineWeber H, Schroeder S, et al. Cell. 181(2):271280.e8. 2020.
10. Huo J, Zhao Y, Ren J, et al. Cell Host Microbe. S19313128(20)303516. 2020.
11. Tai, W., He, L., Zhang, X. et al. Cell Mol Immunol 17, 613–620. 2020.
12. Cao Y, Su B, Guo X, et al. Cell. 182(1):7384.e16. 2020.
13. Premkumar L, SegoviaChumbez B, Jadi R, et al. medRxiv; 2020.
14. Quinlan BD, Mou H, Zhang L, et al. bioRxiv; 2020.
15. Olba NM, Muller MA, Li W, et al. medRxiv; 2020.

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