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AB198092

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

2 Images
Functional Studies - Recombinant human IDH2 protein (DDDDK tag C-Terminus) (AB198092)
  • FuncS

Supplier Data

Functional Studies - Recombinant human IDH2 protein (DDDDK tag C-Terminus) (AB198092)

Activity assay of ab198092.

SDS-PAGE - Recombinant human IDH2 protein (DDDDK tag C-Terminus) (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.

Key facts

Purity

>59% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

DDDDK tag C-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific Activity: 14,200 pmol/min/μg.

Assay Conditions:
The reaction mixture contained 50 mM Tris, pH 7.4, 5 mM MgCl2, 200 μM DL-isocitrate, 200 μM NADP+, and various amount of ab198092 in a volume of 200 μL. Reactions were initiated with the addition of ab198092, and the increase in NADPH absorbance at 340 nm was continuously monitored for 7 min. Molar extinction coefficient of NADPH is 6,220 M-1cm-1.
.

Accession

P48735

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.72% Sodium chloride, 0.71% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MAGYLRVVRSLCRASGSRPAWAPAALTAPTSQEQPRRHYADKRIKVAKPVVEMDGDEMTRIIWQFIKEKLILPHVDIQLKYFDLGLPNRDQTDDQVTIDSALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVADRAGTFKMVFTPKDGSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAIQKKWPLYMSTKNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKSSGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEKVCVETVESGAMTKDLAGCIHGLSNVKLNEHFLNTTDFLDTIKSNLDRALGRQDYKDDDDK","proteinLength":"Full Length","predictedMolecularWeight":"52 kDa","actualMolecularWeight":null,"aminoAcidEnd":452,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Baculovirus infected Sf9 cells","accessionNumber":"P48735","tags":[{"tag":"DDDDK","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Isocitrate dehydrogenase 2 (IDH2) is an enzyme that converts isocitrate to alpha-ketoglutarate in the citric acid cycle through oxidative decarboxylation. IDH2 also known as NADP-dependent isocitrate dehydrogenase has a molecular weight of about 51 kDa. This protein expresses in the mitochondria serving an important role in cellular energy production and intermediary metabolism. By facilitating this conversion IDH2 impacts cellular respiration and energy balance.
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.

The IDH2 protein links to certain cancers like acute myeloid leukemia (AML) due to mutations such as IDH2 R140Q and IDH2 R172K which lead to the production of oncometabolite 2-hydroxyglutarate. This oncometabolite influences epigenetic regulation and cellular differentiation. IDH2 mutations often associate with altered tumor suppressor pathways involving proteins like TP53 contributing to tumorigenesis and impaired cellular differentiation.

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

Product protocols

Target data

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).
See full target information IDH2

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Nature 559:125-129 PubMed29950729

2018

Acquired resistance to IDH inhibition through trans or cis dimer-interface mutations.

Applications

Unspecified application

Species

Unspecified reactive species

Andrew M Intlekofer,Alan H Shih,Bo Wang,Abbas Nazir,Ariën S Rustenburg,Steven K Albanese,Minal Patel,Christopher Famulare,Fabian M Correa,Naofumi Takemoto,Vidushi Durani,Hui Liu,Justin Taylor,Noushin Farnoud,Elli Papaemmanuil,Justin R Cross,Martin S Tallman,Maria E Arcila,Mikhail Roshal,Gregory A Petsko,Bin Wu,Sung Choe,Zenon D Konteatis,Scott A Biller,John D Chodera,Craig B Thompson,Ross L Levine,Eytan M Stein
View all publications

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