Recombinant SARS-CoV-2, RBD Protein (Delta Plus, B1.617.2.1, AY.1, India Variant)

Leinco Technologies
Product Code: LEI-S952
Product Group: Recombinant Proteins
CodeSizePrice
LEI-S952-100ug100 ug£372.00
Quantity:
LEI-S952-500ug500 ug£1,255.00
Quantity:
LEI-S952-1.0mg1.0 mg£2,259.00
Quantity:
Prices exclude any Taxes / VAT

Overview

Host Type: Virus
Regulatory Status: RUO
Shipping:
Ice Packs
Storage:
This recombinant protein may be stored as received at 2-8°C for up to one month. For longer term storage aseptically aliquot in working volumes without diluting and store at -80°C. Avoid Repeated Freeze Thaw Cycles.

Further Information

Concentration:
0.5 mg/ml
Conjugate/Tag/Label:
Purified No Carrier Protein
Format:
This recombinant protein is aseptically packaged and formulated in 0.01 M phosphate buffered saline (PBS) pH 7.2 - 7.4, 150 mM NaCl with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of proteins, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.
Formulation:
This recombinant protein is aseptically packaged and formulated in 0.01 M phosphate buffered saline (PBS) pH 7.2 - 7.4, 150 mM NaCl with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of proteins, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.
Long Description:
The three clades of lineage B.1.617 are B.1.617.1, B.1.617.2, and B.1.617.3, shown in chronological order of detection. This delta plus variant of SARS-CoV-2 (also known as B.1.617.2.1 or AY.1) emerged in India and is spreading in a number of countries.1 The RBD mutation is K417N, L452R, T478K, indicating an extra mutation which distinguishes it from the regular delta variant. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), is an enveloped, single-stranded, positive-sense RNA virus that belongs to the Coronaviridae family 2. The SARS-CoV-2 genome, which shares 79.6% identity with SARS-CoV, encodes four essential structural proteins: the spike (S), envelope (E), membrane (M), and nucleocapsid protein (N) 3. The S protein is a transmembrane, homotrimeric, class I fusion glycoprotein that mediates viral attachment, fusion, and entry into host cells 4. 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 N-terminal (NTD) and C-terminal domains (CTD). The CTD contains the receptor-binding domain (RBD), which binds to the angiotensin-converting enzyme 2 (ACE2) receptor on host cells 4-6. Although both SARS-CoV and SARS-CoV-2 bind the ACE2 receptor, the RBDs only share ~73% amino acid identity, and the SARS-CoV-2 RBD binds with a higher affinity compared to SARS-CoV 4,7. The RBD is dynamic and undergoes hinge-like conformational changes, referred to as the ?down? or ?up? conformations, which hide or expose the receptor-binding motifs, respectively 8. Following receptor binding, S1 destabilizes, and TMPRSS2 cleaves S2, which undergoes a pre- to post-fusion conformation transition, allowing for membrane fusion 9,10.
NCBI Gene:
43740568
Purity:
>95% by SDS Page
Target:
SARS-CoV-2

References

1. Center for Disease Control and Prevention. 2020 2. Zhou, P., Yang, X., Wang, X. et al. Nature 579, 270?273. 2020. 3. Wu, F., Zhao, S., Yu, B. et al. Nature 579, 265?269. 2020. 4. Wrapp D, Wang N, Corbett KS, et al. bioRxiv. 2020.02.11.944462. 2020. 5. Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Cell. 181(2):281-292.e6. 2020. 6. Li W, Zhang C, Sui J, et al. EMBO J. 24(8):1634-1643. 2005. 7. Shang, J., Ye, G., Shi, K. et al. Nature 581, 221?224. 2020. 8. Gui M, Song W, Zhou H, et al. Cell Res. 27(1):119-129. 2017. 9. Walls AC, Tortorici MA, Snijder J, et al. Proc Natl Acad Sci U S A. 114(42):11157-11162. 2017. 10.. Hoffmann M, Kleine-Weber H, Schroeder S, et al. Cell. 181(2):271-280.e8. 2020.

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