AMD1 protein (His tag) (80R-2345)
Purified recombinant Human AMD1 Protein (His tag)
|Synonyms||AMD-1, FLJ26964 protein, DKFZp313L1234 protein, S-adenosylmethionine decarboxylase proenzyme protein, SAMDC protein, AMD 1, ADOMETDC protein, AMD 1 protein, AMD1, AMD protein, AMD-1 protein|
Coomassie Blue stained SDS-PAGE of AMD1 protein (His tag) (80R-2345)
Figure annotation denotes ug of protein loaded and % gel used.
|Residues||MGSSHHHHHH 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|
|Purity||> 80% pure|
|Molecular Weight||33.4 kDa|
|Form & Buffer||Supplied in liquid form in 20mM Tris-HCl buffer (pH 8.0) containing 20% glycerol, 0.1M NaCl, 1mM DTT|
Storage & Safety
|Storage||Store at 4 deg C for short term storage (1-2 weeks). Aliquot and store at -20 deg C to -70 deg C for long term storage. Avoid repeated freeze/thaw cycles.|
|Biological Significance||AMD1 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.|
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