SARS Spike (306-515), Sf9
Sf9, Baculovirus cells.
Spike glycoprotein, S glycoprotein, Peplomer protein, E2 glycoprotein precursor, Severe acute repiratory Syndrome-related Coronavirus, SARS, SRAS-CoV, SARS-CoV1, E2.
Greater than 95.0% as determined by SDS-PAGE.
Description
SARS Spike produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 219 amino acids (306-515 aa) and having a molecular mass of 24.7kDa.
SARS Spike is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
This section provides a brief overview of the SARS Coronavirus and the significance of the Spike (S) protein as a target for research and development of therapeutics.
This part details the characteristics of the SARS Spike protein produced using Sf9 Baculovirus cells, including its amino acid length, molecular weight, attached tag for purification, and purification method.
This section specifies the composition of the solution in which the SARS Spike (306-515) protein is provided. It contains a buffer solution (Phosphate-Buffered Saline) at a specific pH and a cryoprotectant (Glycerol) for storage.
This part provides instructions on how to properly store the SARS Spike (306-515) solution to maintain its stability and activity over time. It includes recommended storage temperatures and advice on long-term storage and avoiding freeze-thaw cycles.
This section states the purity level of the SARS Spike (306-515) protein, which is determined to be greater than 95% based on SDS-PAGE analysis, a technique for separating proteins based on their size.
This part describes how the biological activity of the SARS Spike (306-515) protein is measured. It utilizes a functional ELISA (enzyme-linked immunosorbent assay) to assess its binding ability to the Human ACE-2 protein, which is the receptor for SARS-CoV.
Spike glycoprotein, S glycoprotein, Peplomer protein, E2 glycoprotein precursor, Severe acute repiratory Syndrome-related Coronavirus, SARS, SRAS-CoV, SARS-CoV1, E2.
Sf9, Baculovirus cells.
ADPRVVPSGD VVRFPNITNL CPFGEVFNAT KFPSVYAWER KKISNCVADY SVLYNSTFFS TFKCYGVSAT KLNDLCFSNV YADSFVVKGD DVRQIAPGQT GVIADYNYKL PDDFMGCVLA WNTRNIDATS TGNYNYKYRY LRHGKLRPFE RDISNVPFSP DGKPCTPPAL NCYWPLNDYG FYTTTGIGYQ PYRVVVLSFE LLNAPATVCG PKLHHHHHH
Product Science Overview
The Coronavirus Spike Receptor Binding Domain (RBD) is a critical component of the spike (S) protein of coronaviruses, including SARS-CoV-2, the virus responsible for COVID-19. The RBD is essential for the virus’s ability to infect host cells, as it mediates the binding to the host cell receptor, angiotensin-converting enzyme 2 (ACE2). The specific segment from amino acids 306 to 515 within the spike protein is particularly significant for its role in receptor binding and subsequent viral entry into host cells.
The spike protein of SARS-CoV-2 is a trimeric glycoprotein that protrudes from the viral surface, giving the virus its characteristic crown-like appearance. The RBD within the spike protein is responsible for recognizing and binding to the ACE2 receptor on the surface of host cells. This interaction is the first step in the viral entry process, leading to the fusion of the viral and host cell membranes and the release of the viral genome into the host cell.
The RBD (306-515 a.a.) is a highly conserved region that contains several key residues critical for binding to ACE2. These residues form a binding interface that interacts with the peptidase domain of ACE2, facilitating a strong and specific attachment. The structural integrity of the RBD is maintained by a series of disulfide bonds and a beta-sheet-rich fold, which are essential for its function.
The recombinant production of the RBD (306-515 a.a.) in Sf9 cells involves the use of the baculovirus expression system. Sf9 cells, derived from the fall armyworm Spodoptera frugiperda, are commonly used for the production of recombinant proteins due to their high expression levels and ability to perform post-translational modifications similar to those in mammalian cells.
The process begins with the insertion of the gene encoding the RBD (306-515 a.a.) into a baculovirus vector. This recombinant baculovirus is then used to infect Sf9 cells, leading to the expression of the RBD protein. The expressed protein can be harvested and purified for various applications, including structural studies, vaccine development, and therapeutic research.
The recombinant RBD (306-515 a.a.) has several important applications in the field of virology and immunology. It is used extensively in structural studies to understand the molecular interactions between the virus and the host cell receptor. These studies provide insights into the mechanisms of viral entry and can inform the design of antiviral drugs and vaccines.
In vaccine development, the RBD is a key target for the generation of neutralizing antibodies. Vaccines that elicit a strong immune response against the RBD can effectively block the virus from binding to ACE2, thereby preventing infection. The recombinant RBD is also used in serological assays to detect antibodies in individuals who have been exposed to the virus, aiding in epidemiological studies and vaccine efficacy assessments.
