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Description
SARS-CoV-2 Omicron RBD (BA.2.75), His tagProduct Specification Species SARS CoV 2 Accession P0DTC2 Amino Acid Sequence Protein sequence (P0DTC2, Arg319 Lys537, with C 10*His) RVQPTESIVRFPNITNLCPFHEVFNATRFASVYAWNRKRISNCVADYSVLYNFAPFFAFKCYGVSPTKLNDLCFTNVYADSFVIRGNEVSQIAPGQTGNIADYNYKLPDDFTGCVIAWNSNKLDSKVSGNYNYLYRLFRKSKLKPFERDISTEIYQAGNKPCNGVAGFNCYFPLQSYGFRPTYGVGHQPYRVVVLSFELLHAPATVCGPKKSTNLVKNK Expression System HEK293 Molecular Weight Theoretical: 26. 5kDa Actual: 35kDa Purity 95% by SDS PAGE
Product Specification
| Species | SARS-CoV-2 |
| Accession | P0DTC2 |
| Amino Acid Sequence |
Protein sequence (P0DTC2, Arg319-Lys537, with C-10*His) RVQPTESIVRFPNITNLCPFHEVFNATRFASVYAWNRKRISNCVADYSVLYNFAPFFAFKCYGVSPTKLNDLCFTNVYADSFVIRGNEVSQIAPGQTGNIADYNYKLPDDFTGCVIAWNSNKLDSKVSGNYNYLYRLFRKSKLKPFERDISTEIYQAGNKPCNGVAGFNCYFPLQSYGFRPTYGVGHQPYRVVVLSFELLHAPATVCGPKKSTNLVKNK
|
| Expression System | HEK293 |
| Molecular Weight | Theoretical:26.5kDa Actual:35kDa |
| Purity | ＞95% by SDS-PAGE |
| Endotoxin | <1EU/μg |
| Tag | His Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | Lyophilized from a 0.2 μm filtered solution of 0.2M PBS, pH7.4. |
| Reconstitution | Reconstitute no more than 1 mg/mL according to the size in deionized water after rapid centrifugation. |
| Stability & Storage | 12 months from date of receipt, -20 to -70 °C as supplied. 6 months, -20 to -70 °C under sterile conditions after reconstitution. 1 week, 2 to 8 °C under sterile conditions after reconstitution. Please avoid repeated freeze-thaw cycles. |
Background
Sars-cov-2 (2019-NCOV) infects human respiratory epithelial cells through binding to human ACE2 receptors. Spike protein is a large type I transmembrane protein containing two subunits S1 and S2.S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing cell surface receptors. S2 contains the basic elements required for membrane fusion. S protein plays a key role in inducing neutralizing antibody and T cell responses as well as protective immunity.
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