SARS-CoV-2 (B.1.617.2; AY.1, AY.2, AY.3) Stabilized Spike Glycoprotein (Trimeric), (His-Strep-Tag) is a Fragment protein, in the 16 to 1205 aa range, expressed in HEK 293, with >95% purity and suitable for SDS-PAGE.
>95% SDS-PAGE
HEK 293 cells
His tag C-Terminus
SDS-PAGE
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
SARS-CoV-2 (B.1.617.2; AY.1, AY.2, AY.3) Stabilized Spike Glycoprotein (Trimeric), (His-Strep-Tag) is a Fragment protein, in the 16 to 1205 aa range, expressed in HEK 293, with >95% purity and suitable for SDS-PAGE.
>95% SDS-PAGE
HEK 293 cells
His tag C-Terminus
SDS-PAGE
No
No
pH: 7.4
Constituents: 99% PBS
Fragment
140 kDa
180 kDa
16 to 1205
Recombinant
His tag C-Terminus
Liquid
Dry Ice
-80°C
Avoid freeze / thaw cycle
SARS-CoV-2 Indian (Delta) Variant (B.1.617.2 AY.1 AY.2 AY.3) stabilized spike protein. This varient contains amino acid changes T19R, T95I, G142D, E156G, del157-158, W258L, N417K, L452R, T478K, D614G, P681R, D950N relative to Wuhan-Hu-1.
The protein is stabilized as a pre-fusion trimer due to six amino acid changes in the S2 portion of Spike (HexaPro). The furin cleavage site has been mutated to GSAS and deactivated.
The SARS-CoV-2 Spike Glycoprotein also known as COVID-19 Spike Protein is a trimeric protein weighing approximately 180-200 kDa. It is located on the surface of the SARS-CoV-2 virus playing an important role in virus infectivity. The protein comprises two main subunits S1 and S2 which facilitate attachment to and fusion with host cells. The S1 subunit contains the receptor binding domain (RBD) which specifically binds to the human angiotensin-converting enzyme 2 (ACE2) receptor. The Spike Glycoprotein is expressed in infected host cells mainly in the respiratory tract allowing the virus to enter and initiate replication.
The SARS-CoV-2 Spike Glycoprotein initiates viral entry by interacting with the host cell's ACE2 receptor which leads to viral fusion and entry into the cell's cytoplasm. The protein is part of the virion structure and forms the visible spike on the virion's surface. Upon binding a conformational change triggers the fusion of viral and cellular membranes a vital step for the viral lifecycle. The multimeric nature of the Spike Protein facilitates its interaction with antibodies including those known as 'anti-spike antibodies' which can neutralize the virus and prevent cell infection.
The Spike Glycoprotein plays a significant role in the viral infection process and immune response pathways. It is central to the receptor-mediated endocytosis pathway where the virus is internalized into host cells. The protein’s interaction with ACE2 modifies downstream signaling pathways potentially altering host cell functions. Related proteins in these pathways include the ACE2 receptor and the cellular protease TMPRSS2 which primes the Spike Protein for fusion and viral entry.
The Spike Glycoprotein is chiefly implicated in COVID-19 the disease caused by SARS-CoV-2. The interaction with ACE2 is not just vital for infection but also contributes to the disease's symptomatology as ACE2 is involved in regulating blood pressure and inflammation. Additionally the Spike Protein's role in viral entry makes it a target for therapeutic interventions including 'anti-spike antibodies' and vaccines aimed at blocking this process to prevent infection. The protein's relevance to COVID-19 has led to significant interest in developing diagnostic and therapeutic tools such as 'antibodies COVID' that target the Spike Glycoprotein to manage the disease effectively.
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Reducing SDS-PAGE analysis of ab288550 (2.5 μg).
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