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Merck
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Key Documents

A6888

Sigma-Aldrich

Adenosine 5′-triphosphate–Agarose

aqueous glycerol suspension

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About This Item

MDL number:
MFCD00801332
UNSPSC Code:
23151817
NACRES:
NA.56

form

aqueous glycerol suspension

extent of labeling

≥1 μmol per mL

matrix

cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

ribose hydroxyls

matrix spacer

11 atoms (adipic acid dihydrazide)

storage temp.

−20°C

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Application

Adenosine 5′-triphosphate Agarose (5′-ATP agarose) has been used in affinity chromatography to purify uridine kinase from Ehrlich ascites tumor cells.

Physical form

Suspension in 50% glycerol containing 0.25 M NaCl

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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E Scherzinger et al.
The Journal of biological chemistry, 272(48), 30228-30236 (1997-12-31)
The RepA protein of the mobilizable broad host range plasmid RSF1010 has a key function in its replication. RepA is one of the smallest known helicases. The protein forms a homohexamer of 29,896-Da subunits. A variety of methods were used
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
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
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
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