Sheep Polyclonal Aspartate Aminotransferase antibody - conjugated to HRP. Suitable for Dot and reacts with Pig samples. Immunogen corresponding to Native Full Length Protein corresponding to Pig GOT1.
Preservative: 0.01% Gentamicin sulphate
Constituents: 1% BSA, 0.88% Sodium chloride, 0.424% Potassium phosphate solution
| Dot | |
|---|---|
| Pig | Tested |
| Species | Dilution info | Notes |
|---|---|---|
Species Pig | Dilution info 1/20000 - 1/100000 | Notes - |
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Biosynthesis of L-glutamate from L-aspartate or L-cysteine (PubMed:4634443). Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain (By similarity).
cAspAT, Glutamate oxaloacetate transaminase 1, Transaminase A, cCAT, GOT1
Sheep Polyclonal Aspartate Aminotransferase antibody - conjugated to HRP. Suitable for Dot and reacts with Pig samples. Immunogen corresponding to Native Full Length Protein corresponding to Pig GOT1.
Preservative: 0.01% Gentamicin sulphate
Constituents: 1% BSA, 0.88% Sodium chloride, 0.424% Potassium phosphate solution
Aspartate Transaminase is an IgG fraction antibody purified from monospecific antiserum by a multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against the buffer.
Aspartate Aminotransferase (AST) also known as aspartate transaminase or aspartate transferase is an enzyme important for amino acid metabolism. Mechanically it catalyzes the reversible transfer of an amino group from aspartate to α-ketoglutarate forming oxaloacetate and glutamate. AST has a molecular mass of approximately 92 kDa and is expressed in various tissues with high levels found in liver heart muscle and kidneys. Its presence in these tissues highlights its importance in cellular metabolic processes.
AST facilitates the interconversion between aspartate and oxaloacetate playing a role in the amino acid and urea cycles. Though not part of a large complex AST works closely with similar enzymes such as alanine aminotransferase (ALT) to maintain amino acid balance and support energy production. This enzymatic activity is important in nitrogen metabolism and glutamate use which are necessary for synthesizing other essential molecules within the cell.
AST participates in the citric acid cycle and malate-aspartate shuttle enabling efficient energy production and NADH transport. The enzyme assists in converting oxaloacetate a pivotal intermediate in the citric acid cycle to keep the cycle active ensuring efficient cellular respiration. Additionally in the malate-aspartate shuttle AST works alongside malate dehydrogenase to facilitate the transfer of reducing equivalents across the mitochondrial membrane which is essential for ATP generation.
Elevated AST levels often indicate liver damage such as in hepatitis or cirrhosis reflecting its significant tissue expression. The enzyme is also linked to myocardial infarction as damaged heart muscle releases AST into the bloodstream. In these conditions AST serves as a biomarker for tissue damage often in conjunction with ALT levels allowing clinicians to assess the extent of liver or cardiac injury.
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