A9264
Adenosine 5′-triphosphate–Agarose
lyophilized powder
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About This Item
MDL number:
UNSPSC Code:
41106514
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form
lyophilized powder
extent of labeling
1-5 μmol per mL
matrix
cross-linked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
N-6
matrix spacer
11 atoms
capacity
0.5-2.5 μmol/mL (ATP)
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
Lyophilized powder stabilized with lactose
Storage Class
13 - Non Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Joanna F Swain et al.
The Journal of biological chemistry, 281(3), 1605-1611 (2005-11-09)
The Hsp70 family of molecular chaperones acts to prevent protein misfolding, import proteins into organelles, unravel protein aggregates, and enhance cell survival under stress conditions. These activities are all mediated by recognition of diverse hydrophobic sequences via a C-terminal substrate-binding
R Scaife et al.
The Journal of cell biology, 111(6 Pt 2), 3023-3033 (1990-12-01)
We have purified a 100-kD rat brain protein that has microtubule cross-linking activity in vitro, and have determined that it is dynamin, a putative microtubule-associated motility protein. We find that dynamin appears to be specific to neuronal tissue where it
Purification and characterization of acetate kinase from <I>Clostridium thermocellum</I>.
Lin, W.R., et al.
Tetrahedron, 54, 15915-15925 (1998)
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
Katarzyna Banaszak et al.
Journal of molecular biology, 407(2), 284-297 (2011-01-19)
Phosphofructokinase 1 (PFK) is a multisubunit allosteric enzyme that catalyzes the principal regulatory step in glycolysis-the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate by ATP. The activity of eukaryotic PFK is modulated by a number of effectors in response to
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