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Proteogenix

[Proteogenix] SARS-CoV-2 RBD of Spike protein, K417N, E484K, N501Y – B.1.351 lineage – SA Beta Variant

Cat-No. PX-COV-P053


Proteogenix는 Primary Antibody Biosimilar - Research Grade 

제품을 전문적으로 생산하는 20년의 경험이 있는 High Quality 제조사입니다.




제품 설명 


SARS-CoV-2 RBD of Spike protein, K417N, E484K, N501Y – B.1.351 lineage – SA Beta Variant

 



제품 번호

 

PX-COV-P053

 



제품 특징


Product nameSARS-CoV-2 RBD of Spike protein, K417N, E484K, N501Y - B.1.351 lineage - SA Beta Variant
Origin speciesSARS-COV2
Expression systemEukaryotic expression
Sequence  YP_009724390.1
Molecular weight35kDa
BufferPBS, pH7.5
FormLiquid
Delivery conditionDry Ice
Storage condition4°C for short term; -20°c or -80°C for long term
BrandProteoGenix
Host speciesMammalian cells
ApplicationsELISA,WB
Fragment TypeSpike protein fragment
Aliases /SynonymsRBD of VUI V2 SA variant (V2-202012/01): N501Y, K417N, and E484K, 501.V2 variant, Variant Under Investigation V2 (VUI V2), South African variant, SA variant, B.1.351, Beta variant
ReferencePX-COV-P053
NoteFor research use only. Not suitable for human use.


Description of SARS-CoV-2 RBD of Spike protein, K417N, E484K, N501Y - B.1.351 lineage - SA Beta Variant

General information on SARS-CoV-2 RBD of Spike protein, K417N, E484K, N501Y

The accumulation of mutations K417N, E484K and N501Y in the receptor-binding domain (RBD) of the spike in the new coronavirus, SARS-CoV-2, has been recently described in an emerging variant of the virus. The variant, commonly known as the South African variant or the 501.V2 variant, may have emerged in early August 2020 in Nelson Mandela Bay, South Africa, according to spatiotemporal phylogeographic analysis. However, it was only identified as a Variant of Concern (VOC) by national authorities in mid-December 2020 and has since spread geographically across several provinces and countries.
Observational evidence provided by official authorities in South Africa indicates a potential shift in the clinical epidemiological scenario. Noticeably, clinicians observed a larger proportion of younger patients with no co-morbidities presenting critical illness. Moreover, recent data indicate that variant 501.V2 is the key responsible for causing a resurgence of COVID-19 infections and consequently driving the second wave of the pandemic in this region.
The N501Y mutation had been previously reported in another emerging variant of SARS-CoV-2 known as the B.1.1.7 lineage. This change within the receptor-binding motif (the main functional motif) is known to enhance the binding affinity of the virus to its natural human receptor – ACE2 (angiotensin-converting enzyme 2). ACE2 affinity is expected to be further enhanced by the presence of an additional non-synonymous mutation within this motif, the E484K mutation. This mutation was considered uncommon (less than 0.02% of the sequences outside South Africa) prior to the identification of the 501.V2 variant.
Further analysis of the third key mutation, mutation K417N, indicates this change is expected to have minimal impact on binding affinity to the human ACE2. However, its location is cause for concern. Prior studies indicate that the K417N mutation occurs within the area considered the main target of neutralizing antibodies (NAbs). For this reason, the mutation is expected to abolish interaction with certain NAbs and likely contribute to immune evasion.




QC & Validation Data


SDS-PAGE for SARS-CoV-2 RBD of Spike protein, K417N, E484K, N501Y - B.1.351 lineage - SA Beta Variant





Publications


Winklmeier, S. et al. Persistence of functional memory B cells recognizing SARS-CoV-2 variants despite loss of specific IgG. medRxiv 2021.05.15.21257210. doi: 10.1101/2021.05.15.21257210

- Winklmeier S, Rübsamen H, Özdemir C, Wratil PR, Lupoli G, Stern M, Schneider C, Eisenhut K, Ho S, Wong HK, Taskin D, Petry M, Weigand M, Eichhorn P, Foesel BU, Mader S, Keppler OT, Kümpfel T and Meinl E (2024) Intramuscular vaccination against SARS-CoV-2 transiently induces neutralizing IgG rather than IgA in the saliva. Front. Immunol. 15:1330864. doi: 10.3389/fimmu.2024.1330864




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