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#155104

Anti-GalNAc-T1 [UH3]

Cat. #155104

Anti-GalNAc-T1 [UH3]

Cat. #: 155104

Sub-type: Primary antibody

Unit size: 100 ug

Availability: 10-12 weeks

Target: GalNAc-T1/GALNT1

Class: Monoclonal

Application: ELISA ; IHC ; IF ; IP

Reactivity: Human

Host: Mouse

£300.00

This fee is applicable only for non-profit organisations. If you are a for-profit organisation or a researcher working on commercially-sponsored academic research, you will need to contact our licensing team for a commercial use license.

Contributor

Institute: University of Copenhagen

Tool Details
Target Details
Applications
Handling
References

Tool Details

*FOR RESEARCH USE ONLY (for other uses, please contact the licensing team)

  • Name: Anti-GalNAc-T1 [UH3]
  • Alternate name: UH3, 4D8
  • Research fields: Biochemistry;Cancer;Cell biology
  • Tool sub type: Primary antibody
  • Class: Monoclonal
  • Conjugation: Unconjugated
  • Strain: Balb/c
  • Reactivity: Human
  • Host: Mouse
  • Application: ELISA ; IHC ; IF ; IP
  • Description: GalNAc-T1 is one of many polypeptide GalNAc-transferases that attach GalNAc to proteins forming the GalNAc??1-O-Ser/Thr linkage for GalNAc-type O-glycosylation. The GalNAc-transferase isoforms have considerably overlapping functions as well as unique distinct functions. GalNAc-T1 and –T2 are the main contributors to O-glycosylation of peptides in most cells and they have distinct functions. Murine knock out studies demonstrate that GalNAc-T1 plays important roles in B-cell differentiation. GalNAc-T1 has also been implicated in carcinogenesis. O-glycans are important biomarkers in cancer. The truncated O-glycans comprising Tn formed by the GalNAc transferases and T formed by further elongation by the core1 synthase (C1GalT1) are widely recognized as pancarcinoma antigens. They are masked by sialic acid or further elongation or branching in normal cells. Validation: 1. Positive reaction (IC/IF) in cells expressing GalNAc-T1 using close isoforms as negative controls e.g. GalNAc-T13. 2. Selective IP of active GalNAc-T1 from total cell extracts. 3. Distinct perinuclear staining in cell lines (ICC/IF) and tissues (IHC, IF) suggestive of Golgi localization. 4. loss of staining (IC/IF) following KO of GalNAc-T1
  • Immunogen: Catalytically active secreted GalNAc-T1 produced in insect cells. Recombinant protein containing aa. 41-559 (Uniprot isoform-1)
  • Immunogen uniprot id: Q10472
  • Isotype: IgG1

Target Details

  • Target: GalNAc-T1/GALNT1
  • Target background: GalNAc-T1 is one of many polypeptide GalNAc-transferases that attach GalNAc to proteins forming the GalNAc1-O-Ser/Thr linkage for GalNAc-type O-glycosylation. The GalNAc-transferase isoforms have considerably overlapping functions as well as unique distinct functions. GalNAc-T1 and T2 are the main contributors to O-glycosylation of peptides in most cells and they have distinct functions. Murine knock out studies demonstrate that GalNAc-T1 plays important roles in B-cell differentiation. GalNAc-T1 has also been implicated in carcinogenesis. O-glycans are important biomarkers in cancer. The truncated O-glycans comprising Tn formed by the GalNAc transferases and T formed by further elongation by the core1 synthase (C1GalT1) are widely recognized as pancarcinoma antigens. They are masked by sialic acid or further elongation or branching in normal cells. Validation: 1. Positive reaction (IC/IF) in cells expressing GalNAc-T1 using close isoforms as negative controls e.g. GalNAc-T13. 2. Selective IP of active GalNAc-T1 from total cell extracts. 3. Distinct perinuclear staining in cell lines (ICC/IF) and tissues (IHC, IF) suggestive of Golgi localization. 4. loss of staining (IC/IF) following KO of GalNAc-T1

Applications

  • Application: ELISA ; IHC ; IF ; IP

Handling

  • Format: Liquid
  • Concentration: 0.9-1.1 mg/ml
  • Unit size: 100 ug
  • Storage buffer: PBS with 0.02% azide
  • Storage conditions: -15° C to -25° C
  • Shipping conditions: Dry ice

References

  • A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation.
  • Exploring Regulation of Protein O-Glycosylation in Isogenic Human HEK293 Cells by Differential O-Glycoproteomics.
  • Deconstruction of O-glycosylation--GalNAc-T isoforms direct distinct subsets of the O-glycoproteome.
  • Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness.
  • Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family.
  • Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells.
  • Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family.

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