GOT2 Antibodies
Background
The GOT2 gene encodes mitochondrial aspartic acid aminotransferase, which, as a bifunctional protein, is mainly distributed in the mitochondrial matrix and catalyzes the aminotransfer reaction between aspartic acid and α -ketoglutaric acid. This process not only promotes the energy metabolism of the tricarboxylic acid cycle, but also maintains the REDOX balance between the cytoplasm and mitochondria through the malic acid-aspartic acid shuttle mechanism. Research has found that GOT2 holds a core position in the metabolic regulation of hepatocytes, and its abnormal expression is closely related to urea cycle disorders and various metabolic diseases. The protein structure encoded by this gene was analyzed by X-ray diffraction technology in the 1990s. The specific binding mechanism of its tetramer conformation to the coenzyme pyridoxal phosphate provides an important model for studying the catalytic principles of metabolic enzymes and the energy regulation network of subcellular organelles.
Structure of GOT2
GOT2 is a mitochondrial enzyme protein with a molecular weight of approximately 89 kDa. This protein is composed of 430 amino acid residues and has highly conserved sequence characteristics in different mammals.
| Species | Human | Mouse | Rat | Bovine |
| Molecular Weight (kDa) | 89.2 | 89.1 | 89.3 | 89.0 |
| Primary Structural Differences | Standard sequence | 95% homology | 94% homology | 96% homology |
The tertiary structure of the GOT2 protein presents a typical two-domain conformation: the N-terminal large domain is responsible for catalytic function, while the C-terminal small domain participates in dimer formation. The active center contains highly conserved lysine residues, which bind to the coenzyme pyridoxal phosphate (PLP) through covalent bonds to form a complete transamination catalytic system. The core structure of the four helical bundles of this enzyme remains highly consistent across all species, ensuring the stability of transmembrane transport and metabolic functions.
Fig. 1 Schematic overview of the moonlighting functions of GOT2 in tumor biology.1
Key structural properties of GOT2:
- Typical spatial configuration of the dual domain
- Conservative pyridoxal phosphate (PLP) binding pocket
- Four dimer interface formation of the active center
Functions of GOT2
The core function of the protein encoded by the GOT2 gene is to catalyze the amino transfer reaction between amino acids and keto acids. Its main physiological functions include:
| Function | Description |
| Amino acid metabolism | Catalytic aspartic acid in mitochondria and alpha ketone of glutaric acid amino groups, connect the Krebs cycle and the urea cycle. |
| Malic acid-aspartic acid shuttle | Mediate the transfer of reducing equivalents between the cytoplasm and mitochondria to maintain the REDOX balance of cells. |
| Regulation of energy metabolism | By generating oxaloacetic acid, the tricarboxylic acid cycle flux is affected to ensure the energy supply of cells. |
| Ammonia detoxification assistance | Participate in the ammonia metabolism process of the liver and assist in converting toxic ammonia into non-toxic urea. |
| Metabolic adaptive regulation | Adjust enzyme activity according to nutritional status to adapt to metabolic stress such as hunger and high-protein diet. |
The catalytic efficiency of this enzyme is regulated by both substrate concentration and the mitochondrial NADH/NAD+ ratio. This regulatory mechanism makes it a key node connecting multiple metabolic pathways.
Applications of GOT2 and GOT2 Antibody in Literature
1. Bu, Jiarui, Zeyu Miao, and Qing Yang. "GOT2: New therapeutic target in pancreatic cancer." Genes & Diseases 12.4 (2025): 101370. https://doi.org/10.1016/j.gendis.2024.101370
The article indicates that the current treatments for pancreatic cancer are well tolerated and new targets are urgently needed. Mitochondrial aspartate aminotransferase (GOT2) plays a significant role in the metabolism and immune regulation of pancreatic cancer by maintaining the balance of cellular REDOX and amino acid metabolism, and is expected to become a potential therapeutic target.
2. Hu, Junxi, et al. "GOT2: a moonlighting enzyme at the crossroads of cancer metabolism and theranostics." Frontiers in Immunology 16 (2025): 1626914. https://doi.org/10.3389/fimmu.2025.1626914
The article indicates that GOT2 is a typical part-time enzyme. In addition to catalyzing transamination reactions in mitochondria, it can also regulate fatty acid metabolism and immune gene expression in the nucleus, integrate metabolic and signaling functions, and help tumor cells adapt to stress and achieve immune escape, thus becoming a potential new target for cancer diagnosis and treatment.
3. Kerk, Samuel A., et al. "Metabolic requirement for GOT2 in pancreatic cancer depends on environmental context." Elife 11 (2022): e73245. https://doi.org/10.7554/eLife.73245
The article indicates that in pancreatic cancer, the absence of GOT2 in vitro disrupts the REDOX balance of cells and inhibits proliferation, but in vivo experiments show that its absence does not affect tumor growth. Research has found that cancer-associated fibroblasts help tumor cells reverse metabolic defects caused by GOT2 deficiency by secreting pyruvate, revealing the key role of the tumor microenvironment in metabolic compensation.
4. Yao, Qinfan, et al. "STXBP3 and GOT2 predict immunological activity in acute allograft rejection." Frontiers in Immunology 13 (2022): 1025681. https://doi.org/10.3389/fimmu.2022.1025681
This study found through bioinformatics analysis that GOT2 is highly expressed in patients with acute rejection after kidney transplantation. Verified by RT-qPCR, ELISA and immunohistochemistry, the expression level of GOT2 can reflect the immune status of patients and shows good value in the diagnosis of early acute rejection, and is expected to become a new diagnostic biomarker.
5. Xiong, Yunqiang, et al. "Glucose-induced STUB1-GOT2 axis promotes aspartate synthesis and mitochondrial dysfunction in bladder cancer." Cell Death & Disease 16.1 (2025): 516. https://doi.org/10.1038/s41419-025-07840-5
This study reveals that in bladder cancer, STUB1 inhibits aspartic acid synthesis and mitochondrial function by mediating the ubiquitination modification of GOT2 at the K73 site, reducing its stability. High glucose stress promotes tumor growth through the STUB2-GOT2 axis, which is expected to become a new target for inhibiting the progression of bladder cancer.
Creative Biolabs: GOT2 Antibodies for Research
Creative Biolabs specializes in the production of high-quality GOT2 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.
- Custom GOT2 Antibody Development: Tailor-made solutions to meet specific research requirements.
- Bulk Production: Large-scale antibody manufacturing for industry partners.
- Technical Support: Expert consultation for protocol optimization and troubleshooting.
- Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.
For more details on our GOT2 antibodies, custom preparations, or technical support, contact us at email.
Reference
- Hu, Junxi, et al. "GOT2: a moonlighting enzyme at the crossroads of cancer metabolism and theranostics." Frontiers in Immunology 16 (2025): 1626914. https://doi.org/10.3389/fimmu.2025.1626914
Anti-GOT2 antibodies
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- AActivation
- AGAgonist
- APApoptosis
- BBlocking
- BABioassay
- BIBioimaging
- CImmunohistochemistry-Frozen Sections
- CIChromatin Immunoprecipitation
- CTCytotoxicity
- CSCostimulation
- DDepletion
- DBDot Blot
- EELISA
- ECELISA(Cap)
- EDELISA(Det)
- ESELISpot
- EMElectron Microscopy
- FFlow Cytometry
- FNFunction Assay
- GSGel Supershift
- IInhibition
- IAEnzyme Immunoassay
- ICImmunocytochemistry
- IDImmunodiffusion
- IEImmunoelectrophoresis
- IFImmunofluorescence
- IGImmunochromatography
- IHImmunohistochemistry
- IMImmunomicroscopy
- IOImmunoassay
- IPImmunoprecipitation
- ISIntracellular Staining for Flow Cytometry
- LALuminex Assay
- LFLateral Flow Immunoassay
- MMicroarray
- MCMass Cytometry/CyTOF
- MDMeDIP
- MSElectrophoretic Mobility Shift Assay
- NNeutralization
- PImmunohistologyp-Paraffin Sections
- PAPeptide Array
- PEPeptide ELISA
- PLProximity Ligation Assay
- RRadioimmunoassay
- SStimulation
- SESandwich ELISA
- SHIn situ hybridization
- TCTissue Culture
- WBWestern Blot




