Recombinant humaan AMD1-eiwit

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.

S-adenosylmethionine decarboxylase proenzyme, ADOMETDC, AMD, DKFZp313L1234, FLJ26964, SAMDC

E.coli

Human

His-Tag

SDS-PAGE

0.5 mg/mL (determined by Bradford assay)

> 80% by SDS-PAGE

33.3 kDa (292aa) confirmed by MALDI-TOF

AMD1, S-adenosylmethionine decarboxylase proenzyme, ADOMETDC, AMD, DKFZp313L1234, FLJ26964, SAMDC, ATGP1605-10 µg, ATGP1605-20 µg, ATGP1605-50 µg, ATGP1605-100 µg, ATGP1605-250 µg, ATGP1605-500 µg, ATGP1605-1 mg, ATGP1605-10, ATGP1605-20, ATGP1605-50, ATGP1605-100, ATGP1605-250, ATGP1605-500, ATGP1605-1

Tolbert W.D., et al. (2001) Biochemistry. 40:9484-9494; ; Xiong H., et al. (1999) J. Biol. Chem. 274:35059-35066

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol, 0.1M NaCl, 1mM DTT

Metabolism

NP_001625

P17707

Human

SSMFV 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