Overview
Pepticoater SARS-CoV-2 Complete Wuhan RBD contains a pool of lyophilized peptides selected from the series of 15-mer overlapping peptides, with 11 amino acids overlap, covering the spike glycoprotein (“S”) of SARS Coronavirus-2 Wuhan mutant (GenBank MN908947, Protein QHD43416.1). In particular, this pool consists of the 26 peptides belonging to the Receptor Binding Domain (RBD; amino acids 319-541), which are mutated in the Wuhan strain (B.1.1.529).
Amount: the pool contains 10 μg (approx. 6 nmol) of each peptide (sufficient for stimulation of 1x10
8 cells).
Purity: research-grade, each peptide was individually HPLC purified to a minimum purity of greater than 70% and an average purity of 80% and analysed by LC-HR-MS/MS.
Delivery Format: Each pool is provided freeze-dried in individual vails.
Applications: Antigen specific T-cell stimulation, Immune monitoring, T-cell assays, T-cell expansion.
Additional pools as well as a selection of individual SARS-CoV-2 peptides will be available soon, for more information please inquire using our contact form.
Background information
SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) causes fever, severe respiratory illness and can lead to life threatening pneumonia. The first cases of this disease, termed COVID-19 for coronavirus disease 2019, have been detected in December 2019 in Wuhan, China.
The surface Spike glycoprotein is responsible for the recognition and binding of the coronavirus to the host cell. Once SARS-CoV-2 has bound to the ACE2 receptor of the host cell, fusion of viral envelope and host cell membrane starts, which enables the viral genome to enter the host cell. Thus, the spike protein is crucial for the infection of cells with coronaviruses and has been used as a target for vaccine development.
The spike protein consists of two functional domains: the S1 domain contains the receptor binding domain (RBD) to the ACE2 receptor and the S2 subunit mediates membrane fusion.
This is a joined production with
Intavis Peptide Services and co-developed with the
University of Florence.
