ANTIBODIES

Contributor Information
- Institute University of Copenhagen
Tool Details
- Tool name: Anti-GalNAc-T1 [UH3]
- Alternate names: UH3, 4D8
- Tool type: Antibodies
- Tool sub-type: Primary antibody
- Class: Monoclonal
- Conjugate: Unconjugated
- Reactivity: Human
- Host: Mouse
- Application: ELISA ; IHC ; IF ; IP
- Strain: Balb/c
- Description: GalNAc-T1 is one of many polypeptide GalNAc-transferases that attach GalNAc to proteins forming the GalNAc?ĂÂ?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 ÄËĂÂĂÂT2 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
- Research area: Cancer; Cell biology; Biochemistry
- For Research Use Only
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
Application Details
- Application: ELISA ; IHC ; IF ; IP
Handling
- Format: Liquid
- Concentration: 0.9-1.1 mg/ml
- Storage buffer: PBS with 0.02% azide
- Storage conditions: -15ðC to -25ðC
- Shipping conditions: Shipping at 4ðC
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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.