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L-Methionine y-Lase Polyclonal Antibody
Purified Rabbit Polyclonal Antibody
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- CITATIONS
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- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | P13254 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 42627 Da |
| Other Names | Methionine gamma-lyase, L-methioninase, mdeA |
|---|---|
| Target/Specificity | L-Methionine y-Lase |
| Formulation | 100 µg (0.5 mg/ml) of antibody in PBS pH 7.2, 0.01 % BSA, 0.03 % ProClin®, and 50 % glycerol. |
| Handling | The antibody solution should be gently mixed before use. |
| Background Descriptions | |
| Precautions | L-Methionine y-Lase Polyclonal Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | mdeA {ECO:0000312|EMBL:BAA20553.1} |
|---|---|
| Function | Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia (PubMed:8586629, PubMed:6742420). Is involved in L-methionine catabolism (PubMed:9190812). In fact, shows a multicatalytic function since it also catalyzes gamma-replacement of L-methionine with thiol compounds, alpha,gamma-elimination and gamma-replacement reactions of L- homocysteine and its S-substituted derivatives, O-substituted-L- homoserines and DL-selenomethionine, and, to a lesser extent, alpha,beta-elimination and beta-replacement reactions of L-cysteine, S- methyl-L-cysteine, and O-acetyl-L-serine (PubMed:6742420, PubMed:22785484). Also catalyzes deamination and gamma-addition reactions of L-vinylglycine (PubMed:6742420). Thus, the enzyme is able to cleave C-S, C-Se, and C-O bonds of sulfur, selenium, and oxygen amino acids, respectively (PubMed:6742420, PubMed:22785484). |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Methionine gamma-lyase from Pseudomonas putida is a PLP-dependent enzyme which plays a central role in sulfur amino acid metabolism. METase catalyzes the α, γ-elimination of methionine to α-ketobutyrate, methanethiol, and ammonia. METase also catalyzes the α, γ-elimination of other sulfur containing amino acids, such as homocysteine, cysteine. Because of its ability to deplete methionine, METase has been considered as a viable component of cancer therapeutics against methionine-dependent tumor cells. METase has also been utilized to design drug targets for the infectious diseases caused by parasitic protozoa and anaerobic periodontal bacteria.
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