GCAT Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O75600 |
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Clone Names | 81020113 |
Gene ID | 23464 |
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Other Names | 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial, AKB ligase, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7498c was selected from the Center region of human GCAT. 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 | GCAT (HGNC:4188) |
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Synonyms | KBL |
Function | Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA. |
Cellular Location | Mitochondrion {ECO:0000250|UniProtKB:Q0P5L8}. Nucleus. Note=Translocates to the nucleus upon cold and osmotic stress. |
Tissue Location | Strongly expressed in heart, brain, liver and pancreas. Also found in lung. |
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Provided below are standard protocols that you may find useful for product applications.
Background
The degradation of L-threonine to glycine consists of a two-step biochemical pathway involving the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is first converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. GCAT is the second enzyme in this pathway, which then catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The enzyme is considered a class II pyridoxal-phosphate-dependent aminotransferase.
References
Edgar,A.J., Polak,J.M.Eur. J. Biochem. 267 (6), 1805-1812 (2000)Tressel,T., Thompson,R., J. Biol. Chem. 261 (35), 16428-16437 (1986)
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