AMD1 Protein (His tag)
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- Target See all AMD1 Proteins
- AMD1 (Adenosylmethionine Decarboxylase 1 (AMD1))
- Protein Type
- Recombinant
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This AMD1 protein is labelled with His tag.
- Application
- SDS-PAGE (SDS)
- Purification
- purified by using conventional chromatography.
- Purity
- > 80 % by SDS - PAGE
- Top Product
- Discover our top product AMD1 Protein
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- Comment
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Synonyms: S-adenosylmethionine decarboxylase proenzyme, ADOMETDC, AMD, DKFZp313L1234, FLJ26964, SAMDC
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.5 mg/ml (determined by Bradford assay)
- Buffer
- 20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol, 0.1 M NaCl, 1 MM DTT
- Storage
- 4 °C
- Storage Comment
- Avoid repeated freezing and thawing cycles.
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- Target
- AMD1 (Adenosylmethionine Decarboxylase 1 (AMD1))
- Alternative Name
- AMD1 (AMD1 Products)
- Synonyms
- ADOMETDC Protein, AMD Protein, SAMDC Protein, Amd1a Protein, Amd1b Protein, AMD1 Protein, AdoMetDC Protein, amd Protein, samdc Protein, fb26e03 Protein, si:ch211-257g8.2 Protein, wu:fb26e03 Protein, zgc:55614 Protein, 1 Protein, Amd-1 Protein, SAMDC 1 Protein, adoMetDC1 Protein, CG5029 Protein, Dmel\\CG5029 Protein, l(2)31Dc Protein, l(2)31Dd Protein, l(2)31De Protein, F16B3.10 Protein, F16B3_10 Protein, S-ADENOSYLMETHIONINE DECARBOXYLASE Protein, S-adenosylmethionine decarboxylase Protein, adenosylmethionine decarboxylase 1 Protein, S-adenosylmethionine decarboxylase 1 Protein, S-adenosyl methionine decarboxylase 2 Protein, adenosylmethionine decarboxylase 1 L homeolog Protein, S-adenosylmethionine decarboxylase Protein, AMD1 Protein, Amd1 Protein, amd1 Protein, sam2 Protein, amd1.L Protein, SamDC Protein, SAMDC Protein
- Background
- AMD1, also known as adenosylmethionine decarboxylase proenzyme, is synthesized initially as an inactive 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. Recombinant human AMD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
- Molecular Weight
- 33.4 kDa (292aa) confirmed by MALDI-TOF
- NCBI Accession
- NP_001625
- Pathways
- Ribonucleoside Biosynthetic Process
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