ITN2912
ITN2912
- Catalog: ITN2912
- Gene/Protein: AMD1 AMD
- Product Description: Immunotag™ DCAM Polyclonal Antibody
385.0000
Price in reward points: 385
| Antibody Specification | |
| Datasheet | 
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| Target Protein | DCAM |
| Clonality | Polyclonal |
| Storage/Stability | -20°C/1 year |
| Application | WB,ELISA |
| Recommended Dilution | WB 1:500-2000 ELISA 1:5000-20000 |
| Concentration | 1 mg/ml |
| Reactive Species | H,Rat |
| Host Species | Rabbit |
| Immunogen | Synthesized peptide derived from part region of human protein |
| Specificity | DCAM Polyclonal Antibody detects endogenous levels of protein. |
| Purification | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen |
| Form | Liquid in PBS containing 50% glycerol, and 0.02% sodium azide. |
| Gene Name | AMD1 AMD |
| Accession No. | P17707 P17708 |
| Description | adenosylmethionine decarboxylase 1(AMD1) Homo sapiens This gene encodes an important intermediate enzyme in polyamine biosynthesis. The polyamines spermine, spermidine, and putrescine are low-molecular-weight aliphatic amines essential for cellular proliferation and tumor promotion. Multiple alternatively spliced transcript variants have been identified. Pseudogenes of this gene are found on chromosomes 5, 6, 10, X and Y. [provided by RefSeq, Dec 2013], |
| Cell Pathway/ Category | Cysteine and methionine metabolism,Arginine and proline metabolism, |
| Protein Expression | Heart,Placenta,Prostate,Thymus,Trachea, |
| Subcellular Localization | cytosol, |
| Protein Function | catalytic activity:S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2).,cofactor:Pyruvoyl group.,enzyme regulation:Both proenzyme processing and catalytic activity are stimulated by putrescine. Catalytic activity is inhibited by iodoacetic acid.,pathway:Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.,PTM:Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.,similarity:Belongs to the eukaryotic AdoMetDC family.,subunit:Heterotetramer of two alpha and two beta chains., |
| Usage | For Research Use Only! Not for diagnostic or therapeutic procedures. |
| Material Safety Data Sheet | |
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