B3GNT3抗体;B3GNT3 Antibody—艾普蒂

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-2: Hela and 293T cell lysates, Primary antibody: P12936(B3GNT3 Antibody) at dilution 1/250, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 30 seconds    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P12936(B3GNT3 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P12936(B3GNT3 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

The B3GNT3 antibody targets the β-1.3-N-acetylglucosaminyltransferase 3 (B3GNT3), a glycosyltransferase enzyme involved in synthesizing poly-N-acetyllactosamine (poly-LacNAc) chains on glycoproteins and glycolipids. B3GNT3 catalyzes the transfer of N-acetylglucosamine (GlcNAc) to terminal galactose residues via a β1.3-linkage, a critical step in extending carbohydrate structures implicated in cell adhesion, signaling, and immune recognition. This enzyme is particularly associated with cancer progression, as elevated B3GNT3 expression has been observed in malignancies like colorectal, breast, and ovarian cancers. It contributes to metastasis by facilitating the synthesis of E-selectin ligands, which promote tumor cell adhesion to endothelial cells during hematogenous spread.

B3GNT3 antibodies are essential tools for studying its role in glycosylation-dependent pathological processes. They enable detection and localization of B3GNT3 in tissues or cell lines via techniques such as Western blotting, immunohistochemistry (IHC), or flow cytometry. Research using these antibodies has highlighted B3GNT3's potential as a biomarker for aggressive tumors and a therapeutic target. Inhibiting B3GNT3 activity or expression has shown promise in reducing cancer cell invasiveness in preclinical models. Additionally, B3GNT3 antibodies aid in exploring its regulatory mechanisms, including transcriptional control by oncogenic signaling pathways, further linking aberrant glycosylation to tumor biology.