GOT2 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P00505 |
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Clone Names | 90415087 |
Gene ID | 2806 |
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Other Names | Aspartate aminotransferase, mitochondrial, mAspAT, Fatty acid-binding protein, FABP-1, Glutamate oxaloacetate transaminase 2, Kynurenine aminotransferase 4, Kynurenine aminotransferase IV, Kynurenine--oxoglutarate transaminase 4, Kynurenine--oxoglutarate transaminase IV, Plasma membrane-associated fatty acid-binding protein, FABPpm, Transaminase A, GOT2 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8968a was selected from the N-term region of human GOT2. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | GOT2 (HGNC:4433) |
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Function | Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids. |
Cellular Location | Mitochondrion matrix. Cell membrane. Note=Exposure to alcohol promotes translocation to the cell membrane. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and tricarboxylic acid cycles. The two enzymes are homodimeric and show close homology.
References
Schiele,F., et.al., Clin. Chem. 35 (6), 926-930 (1989)Watazu,Y., et.al., Clin. Chem. 36 (4), 687-689 (1990)
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