Glycine N-Methyltransferase (GNMT) Antibody is a research reagent designed to detect and study the GNMT protein, a key enzyme in methylation metabolism and a tumor suppressor. GNMT catalyzes the transfer of methyl groups from S-adenosylmethionine (SAM/AdoMet) to glycine, producing sarcosine and S-adenosylhomocysteine (SAH). This enzyme regulates the SAM/SAH ratio, influencing methylation-dependent processes such as DNA synthesis, repair, and epigenetic regulation . GNMT antibodies are critical tools for investigating its roles in hepatocellular carcinoma (HCC), immune modulation, and folate metabolism .
GNMT antibodies are utilized in diverse experimental techniques:
GNMT functions as a tumor suppressor in the liver, with its deficiency linked to spontaneous hepatocellular carcinoma (HCC) in mice . Antibody-based studies reveal:
Nuclear localization: GNMT translocates to nuclei in cancer cells, where it suppresses proliferation independently of enzymatic activity .
MYC interaction: GNMT expression is inversely correlated with MYC, a proto-oncogene. Antibodies confirm MYC binds the GNMT promoter, repressing its transcription .
In experimental autoimmune encephalomyelitis (EAE), GNMT deficiency attenuates T-cell responses:
Reduced inflammation: GNMT knockout mice show lower proinflammatory cytokines (IFN-γ, IL-17A) and enhanced regulatory T-cell (Treg) differentiation .
mTOR pathway regulation: GNMT suppresses mTOR signaling in CD4+ T cells, limiting proliferation .
GNMT stabilizes folate-dependent 1-carbon units, supporting nucleotide synthesis and DNA integrity:
Uracil misincorporation: GNMT deficiency increases uracil in DNA during folate depletion, impairing genome stability .
Nucleotide biosynthesis: GNMT enhances purine and pyrimidine synthesis, critical for cell growth and repair .
Nuclear GNMT: Antibody-based IHC shows nuclear GNMT correlates with reduced HCC aggressiveness, suggesting a tumor-suppressive role in the nucleus .
MYC regulation: ChIP assays with GNMT antibodies confirm MYC binds the GNMT promoter, suppressing its expression in cancer .
Treg differentiation: GNMT deficiency enhances Treg cell differentiation in EAE models, mitigating autoimmune inflammation .
mTOR inhibition: GNMT restricts mTOR signaling in CD4+ T cells, limiting proliferation and Th1/Th17 responses .
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Anti-human GNMT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GNMT amino acids 1-295 purified from E. coli.
Glycine N-Methyltransferase is an enzyme that plays a crucial role in the metabolism of amino acids, particularly methionine. It catalyzes the methylation of glycine using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) and S-adenosylhomocysteine (AdoHcy). This reaction is significant in regulating the tissue concentration of AdoMet, which is a key metabolite involved in various cellular processes, including hepatocyte growth, death, and differentiation .
GNMT is predominantly expressed in the liver and is known to be down-regulated in liver cancer tissues. The enzyme’s activity is essential for maintaining normal liver function and preventing the accumulation of toxic metabolites. GNMT deficiency has been linked to several metabolic disorders, including chronic hepatitis, fatty liver, and liver cancer .
The mouse anti human GNMT antibody is a monoclonal antibody that specifically targets the GNMT protein of human origin. This antibody is commonly used in various research applications, including Western blotting, immunoprecipitation, immunofluorescence, immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA). The antibody is typically raised against amino acids 71-295, mapping at the C-terminus of the GNMT protein .
The mouse anti human GNMT antibody is a valuable tool in biomedical research for studying the expression and function of GNMT in different tissues and under various pathological conditions. It helps in understanding the role of GNMT in liver metabolism and its implications in liver diseases. Additionally, this antibody can be used to investigate the molecular mechanisms underlying GNMT-related metabolic disorders and to develop potential therapeutic strategies .
Studies using GNMT knockout mice have provided significant insights into the enzyme’s function. For instance, GNMT-deficient mice exhibit a complete absence of GNMT protein and its activity in the liver, leading to a substantial increase in free methionine and S-adenosylmethionine levels. These mice also develop chronic hepatitis, fatty liver, and liver cancer, highlighting the enzyme’s critical role in liver health .
Moreover, research has shown that GNMT interacts with other proteins, such as Niemann-Pick type C2 protein, affecting cholesterol metabolism and leading to steatohepatitis in GNMT-deficient mice . These findings underscore the importance of GNMT in maintaining metabolic homeostasis and preventing liver diseases.