Antibodies are Y-shaped proteins comprising heavy and light chains, with variable regions (VH, VL) and constant regions (CH, CL) . Their specificity is determined by complementary-determining regions (CDRs) in the variable domains, which bind antigens with high affinity . The Fc region interacts with immune effector cells and the complement system .
Monoclonal antibodies (mAbs) are engineered for high specificity and are used in diagnostics, immunotherapy, and drug delivery . Examples include:
Immunotherapy: Triggers ADCC or inhibits immune checkpoints (e.g., PD-1/PD-L1) .
Disease Prevention: Anti-D antibodies prevent hemolytic disease of the newborn (HDFN) by neutralizing RhD antigens .
Viral Neutralization: SARS-CoV-2 mAbs (e.g., CV07-209) block viral entry by binding the spike protein .
While "LCR23" is not documented, analogous antibodies in research include:
Anti-CD132 mAbs (e.g., REGN7257): Target the IL-2 receptor subunit CD132 to suppress autoimmune responses .
Bispecific Antibodies: Engineered to bind two distinct targets (e.g., FS118 targets PD-L1 and LAG-3) .
Filarial mAbs: Recombinant antibodies (e.g., Ab5B) used for diagnostic quality control or antigen purification .
If LCR23 is a hypothetical or experimental antibody, its design would likely align with these paradigms. For instance:
Target: A cytokine receptor (e.g., CD132), viral protein, or pathogen surface antigen.
Mechanism: Neutralization, immune modulation, or targeted drug delivery.
The absence of LCR23 in literature highlights the need for:
Clarification of Nomenclature: Verify if "LCR23" refers to a specific epitope, protein domain, or proprietary code.
Experimental Validation: In vitro studies to assess binding affinity, epitope mapping, and functional efficacy.
Comparative Analysis: Benchmarking against existing mAbs (e.g., anti-CD132, anti-SARS-CoV-2) to identify unique properties.
KEGG: ath:AT4G29273
STRING: 3702.AT4G29273.1