Description | This product is a human antibody binding to HCMV pentamer composed of gH, gL, UL128, UL130, and UL131A. It bounds solely to the UL proteins at the head of the pentamer. The antibody epitope is solely composed of residues from the membrane-distal tip of UL128. It exhibited neutralization potency against HCMV in this post-attachment assay. |
Clonality | Monoclonal |
Host Species | Human |
Target Species | Human cytomegalovirus (HCMV) |
Epitope | Residues from the membrane-distal tip of UL128 |
Neutralization Mechanism | The antibody competes with NRP2 for binding to the same portion of Pentamer that is engaged by the calcium-coordinating loop of NRP2 domain a2 and disrupt the interaction between Pentamer and NRP2. |
IC50 | 0.0593 nM |
Affinity | KD = 3.11 nM |
Isotype | IgG |
Expression Species | HEK293F or CHO cell |
Purity | >95%, determined by SDS-PAGE and SEC-HPLC |
Endotoxin | <1 EU/mg |
Form | Liquid |
Purification | Protein A purified |
Sterility | 0.2 μM filtered |
Formulation | PBS, pH 7.4 |
Preservation | No preservatives |
Stabilizer | No stabilizers |
Storage | Store at 4°C within one or two weeks. Store at -20°C for long term. Avoid repeated freeze/thaw cycles. Refer to the COA file for specifics. |
Application | SPR; BLI; Neut |
Application Notes | Surface plasmon resonance (SPR): The affinity of antibody for HCMV Pentamer was determined to be 3.11 nM. |
ELISA | Enzyme-Linked Immunosorbent Assay Protocol |
WB | Western Blot Protocol |
FC | Flow Cytometry Protocol |
Target | HCMV Pentamer |
Alternative Name | Human cytomegalovirus pentamer; HCMV pentamer; gH; gL; UL128; UL130; UL131A |
Research Area | Infectious Disease |
Related Disease | Hepatitis, Encephalitis |
Figure 1. Neutralization of antibody 1-103 for both IgG and Fab formats based on inhibition of AD169rev-GFP infection in ARPE-19 cells.
The antibody has potent neutralizing ability against HCMV.
Figure 1. Neutralization of antibody 1-103 for both IgG and Fab formats based on inhibition of AD169rev-GFP infection in ARPE-19 cells.