Anti-HCoV-NL63 Spike S2 antibody [S4897RM] (STJ11104897)
SPECIFICATIONS
ClonalityMonoclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
General Information
| Short Description | Rabbit monoclonal HCoV-NL63 Spike S2 antibody for use in WB and ELISA in hcov-nl63 samples. Datasheet included with dilution recommendations, and related reagents. |
| Applications | WB/ELISA |
| Host | Rabbit |
| Reactivity | HCoV-NL63 |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Clonality | Monoclonal |
| Clone ID | S4897RM |
| Isotype | IgG |
| Conjugation | Unconjugated |
| Concentration | Lot specific |
| Purification | Affinity purification |
| Dilution Range | WB:1:2000-1:20000ELISA:Recommended starting concentration is 1 Mu g/mL. Please optimize the concentration based on your specific assay requirements. |
| Formulation | PBS with 0.05% Proclin300, 0.05% BSA, 50% Glycerol, pH 7.3. |
| Storage Instruction | Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
Target Information
| Specificity | Recombinant protein of human HCoV-NL63 Spike S2. |
Additional Info
| Background | S1 region attaches the virion to the cell membrane by interacting with host ACE2, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. |
Information sourced from Uniprot.org