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A3515

Sigma-Aldrich

Adenosine 2′,5′-diphosphate–Agarose

lyophilized powder

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About This Item

MDL number:
UNSPSC Code:
41106500
NACRES:
NA.56

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

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)


Certificates of Analysis (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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