A3515
Adenosine 2′,5′-diphosphate–Agarose
lyophilized powder
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About This Item
Productos recomendados
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
8 atoms
storage temp.
−20°C
Categorías relacionadas
Application
Adenosine 2′,5′-diphosphate Agarose (2′,5′-ADP agarose) has been used to study NADPH-cytochrome P450 oxidoreductase (CPR), which plays an important role in the insecticide resistance of Anopheles gambiae (a major malaria vector). In particular, Anopheles gambiae CPR (AgCPR) displayed a decreased affinity to adenosine 2′,5′-phosphate when compared to human CPR (hCPR) determined by isothermal titration calorimetry. This may be important for the development of more advanced insecticides that selectively target mosquito CPR.
Physical form
Lyophilized powder stabilized with lactose
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
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Alex Grunau et al.
Biochemistry, 46(28), 8244-8255 (2007-06-22)
A combination of mutagenesis, calorimetry, kinetics, and small-angle X-ray scattering (SAXS) has been used to study the mechanism of ligand binding energy propagation through human cytochrome P450 reductase (CPR). Remarkably, the energetics of 2',5'-ADP binding to R597 at the FAD-binding
Lu-Yun Lian et al.
PloS one, 6(5), e20574-e20574 (2011-06-10)
NADPH-cytochrome P450 oxidoreductase (CPR) plays a central role in chemical detoxification and insecticide resistance in Anopheles gambiae, the major vector for malaria. Anopheles gambiae CPR (AgCPR) was initially expressed in Eschericia coli but failed to bind 2',5'-ADP Sepharose. To investigate
Alex Grunau et al.
Biochemistry, 45(5), 1421-1434 (2006-02-01)
The thermodynamics of coenzyme binding to human cytochrome P450 reductase (CPR) and its isolated FAD-binding domain have been studied by isothermal titration calorimetry. Binding of 2',5'-ADP, NADP(+), and H(4)NADP, an isosteric NADPH analogue, is described in terms of the dissociation
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