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Proteogenix

[Proteogenix] CoV-S[679-833]

Cat-No. PX-COV-P011


Proteogenix는 Primary Antibody Biosimilar - Research Grade 

제품을 전문적으로 생산하는 20년의 경험이 있는 High Quality 제조사입니다.




제품 설명 


CoV-S[679-833]

 



제품 번호

 

PX-COV-P011

 



제품 특징


Product nameCoV-S[679-833]
Origin speciesSARS-COV2
Expression systemProkaryotic expression
SequenceMN908947
Molecular weight19,2kDa
Purity estimated80%
BufferPBS, pH7.5, 4M urea
FormLiquid
Delivery conditionDry Ice
Storage condition4°C for short term; -20°c or -80°C for long term
BrandProteoGenix
Host speciesEscherichia coli (E.coli)
ApplicationsELISA,WB
Fragment TypeSpike protein fragment
Aliases /SynonymsSpike glycoprotein;Spike protein fragment 679-833
ReferencePX-COV-P011
NoteFor research use only. Not suitable for human use.



Description of CoV-S[679-833]

General information on CoV-S [679-833]

Enveloped viruses, such as SARS-CoV-2 the causative agent of COVID-19, enter their host by a process of membrane fusion mediated by a protein exposed in the viral envelop. In the new coronavirus strain, this protein is the spike glycoprotein (protein S) which is a trimeric transmembrane component of the viral envelop. This protein initiates the complex process of receptor binding and membrane fusion, that triggers viral internalization and subsequently the beginning of the virus replication cycle.
Within this protein, several domains play crucial roles in this complex process. In the specific case of SARS-CoV-2, the spike protein is a class I fusion protein which means that after binding the angiotensin-converting enzyme 2 (ACE2) receptor, the protein needs to be primed for fusion by proteolytic cleavage. For this reason, understanding protein cleavage is key to understanding viral pathogenesis in SARS-CoV-2.
The 155 amino acid long region comprised between residues 679 and 833 represents the boundary between the S1 and S2 subunits of the spike glycoprotein in SARS-CoV-2. Researchers have found that the S1/S2 boundary contains a polybasic cleavage site between residues R685 and S686. Furin, a widespread human intracellular protease that recognizes this site, is thus responsible for exposing the fusion domain and initiating viral entry.
The presence of a polybasic cleavage site in this new strain of coronavirus potentially explains its expanded tropism (ability to infect different types of tissue) and increased transmissibility in comparison to SARS-CoV, the virus responsible for the 2003 pandemic.
Designing vaccines or therapeutic antibodies to target this region has the potential of blocking the fusion of the cellular and viral membranes, and subsequently of preventing the infection in its early stages.




QC & Validation Data





Publications


Masih Alam, Rawshan Choudhury, Robert-Jan Lamers, An adaptable in vitro cytokine release assay (CRA): Susceptibility to cytokine storm in COVID-19 as a model, Current Research in Immunology, Volume 3, 2022, Pages 239-243, ISSN 2590-2555, https://doi.org/10.1016/j.crimmu.2022.11.001.




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