CLEC4M抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human gastric cancer tissue using P05687(CLEC4M Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

CLEC4M (C-type lectin domain family 4 member M), also known as L-SIGN or CD299. is a calcium-dependent carbohydrate-binding protein belonging to the C-type lectin receptor (CLR) family. Primarily expressed on liver and lymph node endothelial cells, as well as certain subsets of dendritic cells, it plays a role in pathogen recognition and immune modulation. Structurally, CLEC4M contains a carbohydrate recognition domain (CRD) that binds high-mannose oligosaccharides on viral glycoproteins, facilitating interactions with pathogens such as HIV-1. HCV, SARS-CoV, and Ebola virus. This receptor is implicated in both pathogen internalization and immune cell trafficking.

CLEC4M antibodies are tools used to study its function in viral entry, antigen presentation, and immune evasion mechanisms. Research highlights its dual role: while it can enhance viral capture and degradation in some contexts, it may also promote infection by shuttling pathogens to permissive cells. Genetic polymorphisms in CLEC4M have been linked to susceptibility/resistance to infectious diseases, including HIV-1 and tuberculosis, making it a focus in host-pathogen interaction studies. Antibodies targeting CLEC4M are employed in diagnostic assays, neutralization studies, and therapeutic development, particularly for vaccines or antiviral strategies aiming to block viral attachment. Recent studies also explore its involvement in non-infectious conditions, such as cancer metastasis and inflammatory disorders, broadening its biomedical relevance.