CoV-2 S1 (16-685)
HEK293 Cells.
Spike glycoprotein, S glycoprotein, E2, Peplomer protein, covid19, COVID-19, COVID-19 virus, HCoV-19, Human coronavirus 2019, SARS2, Spike protein S1, Severe acute respiratory syndrome coronavirus 2, 2019-nCoV, S, Peplomer protein
Greater than 85.0% as determined by SDS-PAGE.
Description
The recombinant Coronavirus 2019 CoV-2 Spike Glycoprotein S1, Wuhan-Hu-1 strain containing a total of 680 amino acids (16-685) and having a calculated Mw of 76.2 kDa. CoV-2 S1 (16-685) is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Product Specs
In December 2019, a novel coronavirus responsible for causing viral pneumonia in humans, known as 2019-nCoV or COVID-19, emerged in Wuhan, China. The virus was initially linked to a seafood market.
Genetic analysis revealed that 2019-nCoV shares a high degree of similarity (87%) with SARS-CoV-2, a bat-derived coronavirus discovered in Zhoushan, China, in 2018. Despite some genetic differences, the receptor-binding domain (RBD) of 2019-nCoV closely resembles that of SARS-CoV, suggesting its ability to bind to the human ACE2 receptor (angiotensin-converting enzyme 2).
Bats are considered the likely reservoir of 2019-nCoV. However, researchers believe that an intermediate animal host, potentially present at the seafood market, played a role in transmitting the virus to humans. Studies indicate that 2019-nCoV may be a recombinant virus, with its spike glycoprotein exhibiting characteristics of both bat coronaviruses and an unidentified coronavirus.
This product features the recombinant Coronavirus 2019 (COVID-19) Spike Glycoprotein S1 subunit, specifically from the Wuhan-Hu-1 strain. This protein encompasses amino acids 16 to 685, resulting in a molecular weight of 76.2 kDa. A 6-histidine tag is present at the C-terminus. The protein is purified using advanced chromatographic methods.
This CoV-2 S1 (16-685) solution is provided at a concentration of 0.25mg/ml and is formulated in Phosphate-Buffered Saline (pH 7.4) with 10% Glycerol.
For optimal short-term storage (up to 2-4 weeks), refrigerate the product at 4°C. For extended storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage to maintain protein stability. To preserve protein integrity, minimize repeated freeze-thaw cycles.
The purity of this product is greater than 85.0% as determined by SDS-PAGE analysis.
The biological activity of this product is assessed by its ability to bind to human ACE-2 in a functional ELISA assay.
Spike glycoprotein, S glycoprotein, E2, Peplomer protein, covid19, COVID-19, COVID-19 virus, HCoV-19, Human coronavirus 2019, SARS2, Spike protein S1, Severe acute respiratory syndrome coronavirus 2, 2019-nCoV, S, Peplomer protein
HEK293 Cells.
DGSMVNLTTR TQLPPAYTNS FTRGVYYPDK VFRSSVLHST QDLFLPFFSN VTWFHAIHVS GTNGTKRFDN PVLPFNDGVY FASTEKSNII RGWIFGTTLD SKTQSLLIVN NATNVVIKVC EFQFCNDPFL GVYYHKNNKS WMESEFRVYS SANNCTFEYV SQPFLMDLEG KQGNFKNLRE FVFKNIDGYF KIYSKHTPIN LVRDLPQGFS ALEPLVDLPI GINITRFQTL LALHRSYLTP GDSSSGWTAG AAAYYVGYLQ PRTFLLKYNE NGTITDAVDC ALDPLSETKC TLKSFTVEKG IYQTSNFRVQ PTESIVRFPN ITNLCPFGEV FNATRFASVY AWNRKRISNC VADYSVLYNS ASFSTFKCYG VSPTKLNDLC FTNVYADSFV IRGDEVRQIA PGQTGKIADY NYKLPDDFTG CVIAWNSNNL DSKVGGNYNY LYRLFRKSNL KPFERDISTE IYQAGSTPCN GVEGFNCYFP LQSYGFQPTN GVGYQPYRVV VLSFELLHAP ATVCGPKKST NLVKNKCVNF NFNGLTGTGV LTESNKKFLP FQQFGRDIAD TTDAVRDPQT LEILDITPCS FGGVSVITPG TNTSNQVAVL YQDVNCTEVP VAIHADQLTP TWRVYSTGSN VFQTRAGCLI GAEHVNNSYE CDIPIGAGIC ASYQTQTNSP RRARHHHHHH.
Product Science Overview
The Coronavirus 2019 (COVID-19) pandemic, caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has had a profound impact on global health. One of the key components of SARS-CoV-2 is the spike (S) glycoprotein, which plays a crucial role in the virus’s ability to infect host cells. The spike glycoprotein is a primary target for vaccines and therapeutic interventions due to its essential role in viral entry and its surface exposure, making it accessible to the immune system .
The spike glycoprotein of SARS-CoV-2 is a large type I transmembrane protein that protrudes from the viral envelope. It is composed of two subunits: S1 and S2. The S1 subunit contains the receptor-binding domain (RBD), which is responsible for binding to the angiotensin-converting enzyme 2 (ACE2) receptor on host cells. This binding is the first step in the viral entry process .
The S1 subunit (16-685 amino acids) is particularly significant because it includes the RBD and is the primary target for neutralizing antibodies. The recombinant form of this protein is used in various research and therapeutic applications to study the virus’s interaction with host cells and to develop vaccines and treatments .
The biosynthesis of the spike glycoprotein involves its translation in the endoplasmic reticulum, followed by glycosylation and folding. The protein is then transported to the Golgi apparatus for further processing before being incorporated into the viral envelope. The antigenicity of the spike protein, particularly the S1 subunit, makes it a prime candidate for vaccine development. The immune system recognizes the spike protein, generating an immune response that can neutralize the virus .
Given its crucial role in viral entry, the spike glycoprotein is the focus of most COVID-19 vaccines. Vaccines such as those developed by Pfizer-BioNTech and Moderna use mRNA technology to instruct cells to produce the spike protein, thereby eliciting an immune response. Additionally, monoclonal antibodies targeting the S1 subunit have been developed as therapeutic agents to neutralize the virus in infected individuals .
Recombinant forms of the spike glycoprotein, including the S1 subunit, are widely used in research to understand the virus’s mechanisms of infection and to screen for potential therapeutic compounds. These recombinant proteins are produced using various expression systems, such as mammalian cells, to ensure proper folding and glycosylation, which are critical for maintaining their functional and antigenic properties .
