Diamine Nacetyltransferase 1 protein (His tag) (80R-1181)
Purified recombinant Human Diamine Nacetyltransferase 1 protein
|Synonyms||Putrescine acetyltransferase protein, SAT1 protein, SAT protein, Polyamine N-acetyltransferase 1 protein, Diamine acetyltransferase 1 protein, SSAT-1 protein, Diamine Nacetyltransferase -1 protein, SSAT 1., Diamine Nacetyltransferase 1, EC 18.104.22.168 protein, Spermidine/spermine N(1)-acetyltransferase 1 protein, spermidine/spermine N1-acetyltransferase 1 protein, DC21 protein, Diamine Nacetyltransferase 1, Diamine Nacetyltransferase -1, SSAT protein, Diamine Nacetyltransferase 1 protein, KFSD protein, KFSDX protein|
Coomassie Blue stained SDS-PAGE of Diamine Nacetyltransferase 1 protein (His tag) (80R-1181)
Figure annotation denotes ug of protein loaded and % gel used.
|Residues||1-171 amino acids: MGSSHHHHHH SSGLVPRGSH MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP FYHCLVAEVP KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMRC RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMATE E|
|Purity||> 95% pure|
|Molecular Weight||22.1 kDa (191aa), confirmed by MALDI-TOF.|
|Form & Buffer||Supplied as a liquid in 20mM Tris-HCl buffer, pH 8.0, containing 10% glycerol.|
Storage & Safety
|Storage||Store at 4 deg C for short term storage (1/2 weeks). Aliquot and store at -20 deg C or - 70 deg C for long term storage. Avoid repeated freeze/thaw cycles.|
|Biological Significance||Diamine N-acetyltransferase 1 (or Spermidine/spermine-N1-acetyltransferase, SSAT1), also known as SAT-1, is a polyamine catabolic enzyme which catalyzes the acetylation of polyamines. This protein plays an important role in polyamine homoeostasis, since acetylated products are either excreted from the cell or oxidized by acetylpolyamine oxidase. A variety of other effects of increased SAT-1 activity include death of pancreatic cells, blockage of regenerative tissue growth, behavioral changes, keratosis follicularis spinulosa decalvans(KFSD), and hair loss. Recombinant human SAT-1, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography.|
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