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Human IDH1 (R132C) Protein, His Tag (MALS verified)

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ID1-H51H8-20ug
$360.00
In Stock - Delivery in 1-2 business days
ID1-H51H8-100ug
$1,010.00
In Stock - Delivery in 1-2 business days
ID1-H51H8-500ug
$3,605.00
In Stock - Delivery in 2-3 weeks
ID1-H51H8
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Synonyms

IDH1, PICD, IDP

Source

Human IDH1 (R132C), His Tag (ID1-H51H8) is expressed from E. coli cells. It contains AA Met 1 - Leu 414 (Accession # O75874-1(R132C)).

Predicted N-terminus: Met 1

Molecular Characterization
Other Tags and Version Biotin & Other Labeled Version

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 48.5 kDa. The protein migrates as 47-50 kDa under reducing (R) condition (SDS-PAGE).

The protein is designed as a dimer.

Purity

>95% as determined by SDS-PAGE.

Formulation

Supplied as 0.2 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5 with glycerol as protectant.

Contact us for customized product form or formulation.

Shipping and Storage

This product is supplied and shipped on dry ice.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • The product MUST be stored at -70°C or lower upon receipt;
  • -70°C for 3 months under sterile conditions.
ACRO Quality Management System

Introduction de fond

The IDH enzymes catalyze the oxidative decarboxylation of isocitrate to alpha-ketoglutarate (α-KG), producing nicotinamide adenine dinucleotide phosphate (NADPH) in the process via the citric acid cycle. Eukaryotic cells express two distinct classes of IDHs that utilize either NAD or NADP as their cofactors and serve diverse biological functions. NAD-dependent IDH is localized to the mitochondrial matrix and is well known for its central role for energy production in the Krebs cycle. NADP-dependent IDHs are primarily located either in mitochondria or cytoplasm . Each NADP-dependent isozyme is a homodimer. Mutations of Arg132 of human IDH1 result in a reduced ability of the enzyme to convert isocitrate to alpha ‑ketoglutarate, but the enzyme acquires the ability to generate 2-hydroxyglutarate (2HG) from alpha‑ketoglutarate，2-HG is elevated in several tumor types, including a subset of AMLs.