Recombinant human IDH2 protein (DDDDK tag C-Terminus)
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(1 Publication)
Recombinant human IDH2 protein (DDDDK tag C-Terminus) is a Human Full Length protein, in the 1 to 452 aa range, expressed in Baculovirus infected Sf9 cells, with >59%, suitable for SDS-PAGE, FuncS.
View Alternative Names
IDH, ICD-M, IDP, NADP(+)-specific ICDH, Oxalosuccinate decarboxylase, IDH2
- FuncS
Supplier Data
Functional Studies - Recombinant human IDH2 protein (DDDDK tag C-Terminus) (AB198092)
Activity assay of ab198092.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human IDH2 protein (DDDDK tag C-Terminus) (AB198092)
10% SDS-PAGE analysis of 1.4 μg ab198092 with Coomassie staining.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The IDH2 enzyme facilitates cellular metabolism by producing NADPH critical for biosynthesis and antioxidant defense. It functions within the oxidative decarboxylation of isocitrate providing reducing equivalents to keep cellular redox balance. Although not part of a larger enzymatic complex IDH2 acts synergistically with other metabolic enzymes to maintain cellular biochemical pathways.
Pathways
The IDH2 protein participates in the citric acid cycle and redox homeostasis. IDH2 contributes to the tricarboxylic acid (TCA) pathway coupling with other TCA components such as citrate synthase and aconitase. Within the redox pathway it influences glucose metabolism via its link with enzymes like NADPH oxidase ensuring a steady supply of NADPH for biosynthetic reactions.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Plays a role in intermediary metabolism and energy production (PubMed : 19228619, PubMed : 22416140). It may tightly associate or interact with the pyruvate dehydrogenase complex (PubMed : 19228619, PubMed : 22416140).
Sequence similarities
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Post-translational modifications
Acetylation at Lys-413 dramatically reduces catalytic activity. Deacetylated by SIRT3.
Subcellular localisation
Mitochondrion
Target data
Publications (1)
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Nature 559:125-129 PubMed29950729
2018
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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