Anti-Human MUC1 Recombinant Antibody (TAB-173)

CAT#: TAB-173

Recombinant monoclonal antibody to MUC1. It is a humanized monoclonal antibody designed for the treatment of cancers. The antibody is linked to a cytotoxic agent, ravtansine.

Gene Expression
Figure 1 IF staining of human cell line RPTEC TERT1 Figure 2 IHC staining of human stomach Figure 3 IF staining of human cell line A-431 Figure 4 IF staining of human cell line U-2 OS Figure 5 Stomach Figure 6 Colon Figure 7 Kidney Figure 8 Testis Figure 9 RNA cell line category: Group enriched (CAPAN-2, OE19, RPTEC TERT1, T-47d)

Specifications

  • Immunogen
  • Synthetic peptide, corresponding to residues from the C-terminus of Human MUC1.
  • Host Species
  • Mouse
  • Derivation
  • Humanized (from mouse)
  • Type
  • IgG1 - kappa
  • Specificity
  • Tested positive against native human antigen.
  • Species Reactivity
  • Human
  • Applications
  • Suitable for use in IF, IP, Neut, FuncS, ELISA, FC, ICC and most other immunological methods.
  • Related Disease
  • Gastric cancers (metastatic or locally advanced)

Product Property

  • Purity
  • >95.0% as determined by Analysis by RP-HPLC & analysis by SDS-PAGE.
  • Storage
  • Store it under sterile conditions at -20°C upon receiving. Recommend to pack the protein into smaller quantities for optimal storage.

Target

  • Alternative Names
  • Cantuzumab ravtansine;868747-45-9;C242-DM4;huC242-SPDB-DM4;MUC1;mucin 1, cell surface associated;mucin 1, transmembrane , PUM;mucin-1;CD227;PEM;episialin;DF3 antigen;H23 antigen;krebs von den Lungen-6;mucin 1, transmembrane;tumor-associated mucin;carcinom
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Citations

  1. Wu, Zhengliang L., et al. "Detecting substrate glycans of fucosyltransferases with fluorophore-conjugated fucose and methods for glycan electrophoresis." Glycobiology 30.12 (2020): 970-980. https://doi.org/10.1093/glycob/cwaa030
    This study introduces a novel method for detecting substrate glycans of fucosyltransferases using fluorophore-conjugated fucose and gel electrophoresis techniques. The researchers demonstrated that various fucosyltransferases (FUT2, FUT6, FUT7, FUT8, and FUT9) can recognize and transfer fluorophore-conjugated fucose to their substrate glycans on glycoproteins. This approach allowed for the visualization and characterization of substrate glycans on fetal bovine fetuin, recombinant H1N1 viral neuraminidase, and therapeutic antibodies. The study established electrophoresis-based methods for analyzing free glycans, enabling the researchers to track the enzymatic synthesis of Lewis X and sialyl Lewis X structures. Importantly, the research revealed that fucosylation occurs at a much faster rate than sialylation, suggesting that fucosyltransferases are key regulatory targets in the synthesis of these important glycan epitopes.
    Creative Biolabs provided Cantuzumab, an anti-Muc1 therapeutic antibody that lacks core-6 fucosylation. This antibody served as a critical test substrate for demonstrating FUT8's ability to incorporate fluorophore-conjugated fucose into substrate glycans, particularly for comparing glycan structures between antibodies with and without core fucosylation. The availability of this specialized therapeutic antibody enabled the researchers to clearly identify and characterize the substrate specificities of different fucosyltransferases, which has important implications for understanding glycan epitope regulation and potentially for developing targeted therapeutic interventions.

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Product Notes

This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:

• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production

See more details about Hi-Affi™ recombinant antibody benefits.

Datasheet

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Protocol & Troubleshooting

We have outlined the assay protocols, covering reagents, solutions, procedures, and troubleshooting tips for common issues in order to better assist clients in conducting experiments with our products. View the full list of Protocol & Troubleshooting.

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