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Merck

A3515

Sigma-Aldrich

Adenosine 2′,5′-diphosphate–Agarose

lyophilized powder

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About This Item

MDL號碼:
分類程式碼代碼:
41106500
NACRES:
NA.56

形狀

lyophilized powder

標籤範圍

1-5 μmol per mL

基質

cross-linked 4% beaded agarose

基質活化

cyanogen bromide

基質結合

N-6

基質墊片

8 atoms

儲存溫度

−20°C

相关类别

應用

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.

外觀

用乳糖稳定化的冻干粉

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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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, 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
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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