• Western blot analysis of recombinant Human coronavirus (HCoV-NL63) Spike Protein (S1+S2 ECD His Tag) using HCoV-NL63 Spike S2 Rabbit monoclonal antibody (STJ11104897) at 1:20000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (STJS000856) at 1:10000 dilution. NA NA Lysates/proteins: 10ng per lane. NA NA Blocking buffer: 3% nonfat dry milk in TBST. NA NA Detection: ECL Basic Kit. NA NA Exposure time: 60s.

Anti-HCoV-NL63 Spike S2 antibody [S4897RM] (STJ11104897)

SKU:
STJ11104897

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Host: Rabbit
Applications: WB
Reactivity: HCoV-NL63
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit monoclonal antibody anti-HCoV-NL63 Spike S2 is suitable for use in Western Blot research applications.
Clonality: Monoclonal
Clone ID: S4897RM
Conjugation: Unconjugated
Isotype: IgG
Formulation: PBS with 0.05% Proclin300, 0.05% BA, 50% Glycerol, pH7.3.
Purification: Affinity purification
Dilution Range: WB 1:2000-1:20000
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Immunogen: Recombinant protein of human HCoV-NL63 Spike S2.
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

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