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Adenosine 5′-triphosphate Agarose (5′-ATP agarose) has been used in affinity chromatography to purify uridine kinase from Ehrlich ascites tumor cells.
物理的形状
50%グリセロ-ル懸濁液(0.25M NaCl含有)
保管分類コード
10 - Combustible liquids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
A6888-5ML:
A6888-BULK:
A6888-VAR:
A6888-1ML:
A6888-10ML:
最新バージョンのいずれかを選択してください：
試験成績書（COA）
Lot/Batch Number
B L Stitt
The Journal of biological chemistry, 263(23), 11130-11137 (1988-08-15)
We have determined that 3 mol of ATP or other adenine nucleotide can bind to Escherichia coli transcription termination protein rho, in the presence or absence of the RNA cofactor that is required for activation of rho's ATPase activity. Isotope
S Ogg et al.
The Journal of biological chemistry, 269(48), 30461-30469 (1994-12-02)
Human Cdc25C is a protein phosphatase that dephosphorylates and activates Cdc2-cyclin B to trigger entry into mitosis. Cdc25C is itself regulated by phosphorylation. In asynchronously growing HeLa cells, we have determined that serine 216 is the major site of Cdc25C
V Nagaraja et al.
Journal of molecular biology, 182(4), 579-587 (1985-04-20)
We have purified the type I restriction enzymes SB and SP from Salmonella typhimurium and S. potsdam, respectively, and determined the DNA sequences that they recognize. These sequences resemble those previously determined for the type I enzymes, EcoB, EcoK and
H D Kim et al.
Biochemistry, 38(44), 14697-14710 (1999-11-05)
Two polynucleotide-dependent ATPases, 95 and 181 kDa in size, have been purified to near homogeneity from cell-free extracts of Schizosaccharomyces pombe. Despite their size differences, their biochemical properties were strikingly similar. Both enzymes were capable of unwinding RNA and DNA
B Suri et al.
The EMBO journal, 3(3), 575-579 (1984-03-01)
The EcoA restriction enzyme from Escherichia coli 15T- has been isolated. It proves to be an unusual enzyme, clearly related functionally to the classical type I restriction enzymes. The basic enzyme is a two subunit modification methylase. Another protein species
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