A6888
Adenosine 5′-triphosphate–Agarose
aqueous glycerol suspension
Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
About This Item
form
aqueous glycerol suspension
Quality Level
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
SMILES string
[X]Nc1ncnc2[n](cnc21)[C@@H]3O[C@@H]([C@H]([C@H]3O)O)CO[P](=O)(O[P](=O)(O[P](=O)(O)O)O)O
Looking for similar products? Visit Product Comparison Guide
Related Categories
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
flash_point_f
Not applicable
flash_point_c
Not applicable
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
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
Yasuo Nakahara et al.
Journal of basic microbiology, 44(6), 459-470 (2004-11-24)
UDPgalactose:polysaccharide galactosyl-transferase is the enzyme that is specifically localized in prespore cells of Dictyostelium discoideum and its activity sharply changes in response to differentiation and dedifferentiation. To clarify the nature of this enzyme, we first developed an improved assay method
Global Trade Item Number
| SKU | GTIN |
|---|---|
| A6888-5ML | 04061837769580 |
| A6888-1ML | 04061837769573 |
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service