SARS-CoV-2 RBD of Spike protein–BA.4 lineage B.1.1.529.4 – Omicron Variant

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Product nameSARS-CoV-2 RBD of Spike protein–BA.4 lineage B.1.1.529.4 – Omicron Variant
Origin speciesSARS-COV2
Expression systemEukaryotic expression
Sequence  YP_009724390.1
Molecular weight35kDa
BufferPBS, pH7.5
Delivery conditionDry Ice
Storage condition4°C for short term; -20°c or -80°C for long term
BrandProteoGenix
Host speciesMammalian cells
Fragment TypeSpike protein fragment
Aliases /SynonymsB.1.1.529.4, Omicron variant, BA.4
ReferencePX-COV-P078
NoteFor research use only. Not suitable for in vitro diagnostic and human use.

Description of SARS-CoV-2 RBD of Spike protein–BA.4 lineage B.1.1.529.4 – Omicron Variant

The Structure of SARS-CoV-2 RBD of Spike protein–BA.4 lineage B.1.1.529.4 – Omicron Variant

The SARS-CoV-2 RBD (receptor-binding domain) of Spike protein–BA.4 lineage B.1.1.529.4 – Omicron Variant is a key component of the virus responsible for the COVID-19 pandemic. This variant, also known as the Omicron variant, was first identified in South Africa in November 2021 and has since spread to multiple countries around the world. Understanding the structure of this variant’s RBD is crucial in developing effective treatments and vaccines against COVID-19.

The RBD is a small, compact protein located on the surface of the SARS-CoV-2 virus. It is responsible for binding to the ACE2 receptor on human cells, allowing the virus to enter and infect the cell. The RBD is made up of 193 amino acids and has a unique three-dimensional structure that is essential for its function.

The Omicron variant has several mutations in its RBD compared to the original SARS-CoV-2 virus. These mutations, including N440K, G446S, S477N, Q493R, and Q498R, are located in key regions of the RBD that interact with the ACE2 receptor. This altered structure of the RBD may explain the increased transmissibility of the Omicron variant compared to previous variants.

The Activity of SARS-CoV-2 RBD of Spike protein–BA.4 lineage B.1.1.529.4 – Omicron Variant

The activity of the RBD is crucial for the infection and spread of the SARS-CoV-2 virus. The mutations in the RBD of the Omicron variant have been shown to increase its binding affinity to the ACE2 receptor, making it easier for the virus to enter and infect cells. This increased binding affinity may contribute to the increased transmissibility of the Omicron variant.

Furthermore, the RBD is also a target for neutralizing antibodies produced by the immune system in response to infection or vaccination. The mutations in the RBD of the Omicron variant may also affect the binding of these antibodies, potentially reducing their effectiveness in neutralizing the virus. This highlights the importance of ongoing research to understand the impact of these mutations on the activity of the RBD and the effectiveness of current treatments and vaccines.

The Application of this protein

The structure and activity of the RBD of the Omicron variant have significant implications for the development of treatments and vaccines against COVID-19. Understanding the specific mutations in the RBD can aid in the design of targeted therapeutics that can effectively block the binding of the virus to the ACE2 receptor. This could potentially reduce the severity of the disease and prevent its spread.

Additionally, the RBD is a key antigen in many COVID-19 vaccines, and the mutations in the Omicron variant may affect the efficacy of these vaccines. Ongoing research is needed to determine if booster shots or new vaccine formulations are necessary to provide protection against this variant.

In conclusion, the SARS-CoV-2 RBD of Spike protein–BA.4 lineage B.1.1.529.4 – Omicron Variant is a critical component of the virus responsible for the COVID-19 pandemic. Its unique structure and activity have significant implications for the development of effective treatments and vaccines against this highly transmissible variant. Ongoing research and surveillance are crucial in understanding and combating the Omicron variant and other emerging variants of the SARS-CoV-2 virus.

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