AMD1 Recombinant Protein
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| Amount : | 5 µg |
| Purification : | Greater than 80% as determined by SDS-PAGE. |
| Content : | The AMD1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol. |
| Storage condition : | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. |
| AA sequence : | GSSHHHHHH SSGLVPRGSH MGSHMSSMFV SKRRFILKTC GTTLLLKALV PLLKLARDYS GFDSIQSFFY SRKNFMKPSH QGYPHRNFQE EIEFLNAIFP NGAAYCMGRM NSDCWYLYTL DFPESRVISQ PDQTLEILMS ELDPAVMDQF YMKDGVTAKD VTRESGIRDL IPGSVIDATM FNPCGYSMNG MKSDGTYWTI HITPEPEFSY VSFETNLSQT SYDDLIRKVV EVFKPGKFVT TLFVNQSSKC RTVLASPQKI EGFKRLDCQS AMFNDYNFVF TSFAKKQQQQ QS |
| Alternative Name : | Adenosylmethionine decarboxylase 1, S-adenosylmethionine decarboxylase proenzyme, AdoMetDC, S-adenosylmethionine decarboxylase 1, SAMDC, AMD, EC 4.1.1.50. |
Source : E.coli.
AMD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (68-334) and having a molecular mass of 33.4 kDa.AMD1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Adenosylmethionine decarboxylase proenzyme (AMD1) is synthesized originally as an inactive proenzyme. Putrescine stimulates both the proenzyme processing and the catalytic activity. The catalytic activity is inhibited by iodoacetic acid. The active enzyme formation entails a self-maturation process in which the active site pyruvoyl group is produced from an internal serine residue using an autocatalytic post-translational modification.
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