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IDH1 (R132H), FLAG-tag Recombinant
IDH1 (R132H), FLAG-tag Recombinant
Artikelnummer
BPS71099-1
Verpackungseinheit
50 µg
Hersteller
BPS Bioscience
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Applications: Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Assay Conditions: IDH reductive activity was measured in 200 µl reaction containing 25 mM Tris (pH 7.4), 150 mM NaCl, 10 mM MgCl2, 0.03% BSA, 1 mM alpha-Ketoglutarate, 10 ?M NADPH and IDH. Depletion of NADPH was monitored continuously at Abs340 nm for 20 min. Molar extinction coefficient of NADPH is 6,200 M-1cm-1.
Background: Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). IDH1 homodimer is an NADP(+)-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. It contains the PTS-1 peroxisomal targeting signal sequence. The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, as well as in peroxisomal reactions that consume 2-oxoglutarate. The cytoplasmic enzyme serves a significant role in cytoplasmic NADPH production.
Description: Human Isocitrate Dehydrogenase (IDH1), also known as oxalosuccinate decarboxylase, GenBank Accession No. NM_005896, full length [a.a. 1-414(end)] with Arg to His mutation on a.a. 132 and C-terminal FLAG-tag, MW= 48 kDa, expressed in Sf9 cells via a baculovirus expression system.
Format: Aqueous buffer solution
Formulation: 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 80 µg/ml FLAG peptide, 0.04% Tween-20 and 20% glycerol.
Genbank: NM_005896
Storage Stability: At least 6 months at -80°C.
Tags: C-terminal FLAG-tag
Uniprot: O75874
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. Dang, L., et al. (2010). Trends Mol. Med. 16(9):387-97.
2. Paschka, P., et al. (2010). J. Clin. Oncol. 28(22):3636-43.
Applications: Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Assay Conditions: IDH reductive activity was measured in 200 µl reaction containing 25 mM Tris (pH 7.4), 150 mM NaCl, 10 mM MgCl2, 0.03% BSA, 1 mM alpha-Ketoglutarate, 10 ?M NADPH and IDH. Depletion of NADPH was monitored continuously at Abs340 nm for 20 min. Molar extinction coefficient of NADPH is 6,200 M-1cm-1.
Background: Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). IDH1 homodimer is an NADP(+)-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. It contains the PTS-1 peroxisomal targeting signal sequence. The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, as well as in peroxisomal reactions that consume 2-oxoglutarate. The cytoplasmic enzyme serves a significant role in cytoplasmic NADPH production.
Description: Human Isocitrate Dehydrogenase (IDH1), also known as oxalosuccinate decarboxylase, GenBank Accession No. NM_005896, full length [a.a. 1-414(end)] with Arg to His mutation on a.a. 132 and C-terminal FLAG-tag, MW= 48 kDa, expressed in Sf9 cells via a baculovirus expression system.
Format: Aqueous buffer solution
Formulation: 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 80 µg/ml FLAG peptide, 0.04% Tween-20 and 20% glycerol.
Genbank: NM_005896
Storage Stability: At least 6 months at -80°C.
Tags: C-terminal FLAG-tag
Uniprot: O75874
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. Dang, L., et al. (2010). Trends Mol. Med. 16(9):387-97.
2. Paschka, P., et al. (2010). J. Clin. Oncol. 28(22):3636-43.
| Artikelnummer | BPS71099-1 |
|---|---|
| Hersteller | BPS Bioscience |
| Hersteller Artikelnummer | 71099-1 |
| Green Labware | Nein |
| Verpackungseinheit | 50 µg |
| Mengeneinheit | STK |
| Produktinformation (PDF) | Download |
| MSDS (PDF) |
|
Immer für Sie da
Gernot Ensinger, M.Sc.
Laurent Haze
