OGDC-E Protein, Mouse (His-SUMO)

The OGDC-E Protein, a vital component of the 2-oxoglutarate dehydrogenase complex, drives the conversion of 2-oxoglutarate to succinyl-CoA in the mitochondrion, a pivotal step in the Krebs cycle.It employs thiamine diphosphate for decarboxylation, connecting to the E2 enzyme and participating in nuclear histone succinylation with KAT2A.OGDC-E Protein, Mouse (His-SUMO) is the recombinant mouse-derived OGDC-E protein, expressed by E.coli , with N-SUMO, N-6*His labeled tag.

The OGDC-E protein is a component of the 2-oxoglutarate dehydrogenase complex (OGDHC), specifically the E1o component. It plays a crucial role in the first and rate-limiting step of converting 2-oxoglutarate to succinyl-CoA and CO(2) within the OGDHC. This conversion is catalyzed by the entire OGDHC. The OGDC-E protein facilitates the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) using the thiamine diphosphate (ThDP) cofactor. It then transfers the decarboxylated acyl intermediate to an oxidized dihydrolipoyl group that is covalently linked to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). This process occurs in the mitochondrion and is a critical step in the Krebs (citric acid) cycle, which is a common pathway for oxidizing fuel molecules such as carbohydrates, fatty acids, and amino acids. While the OGDC-E protein can catalyze the decarboxylation of 2-oxoadipate in vitro, it does so at a much slower rate compared to 2-oxoglutarate. Additionally, a fraction of the 2-oxoglutarate dehydrogenase complex localizes in the nucleus and is involved in lysine succinylation of histones. It associates with KAT2A on chromatin and supplies succinyl-CoA to the histone succinyltransferase KAT2A.

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Mouse

E. coli

N-SUMO;N-6*His

Q60597 (V695-S1023)

18293  [NCBI]

Partial

VDKRTCIPMNHLWPNQAPYTVCNSSLSEYGVLGFELGFAMASPNALVLWEAQFGDFNNMAQCIIDQFICPGQAKWVRQNGIVLLLPHGMEGMGPEHSSARPERFLQMCNDDPDVLPDLQEENFDINQLYDCNWIVVNCSTPGNFFHVLRRQILLPFRKPLIVFTPKSLLRHPEARTSFDEMLPGTHFQRVIPENGPAAQDPHKVKRLLFCTGKVYYDLTRERKARNMEEEVAITRIEQLSPFPFDLLLKEAQKYPNAELAWCQEEHKNQGYYDYVKPRLRTTIDRAKPVWYAGRDPAAAPATGNKKTHLTELQRFLDTAFDLDAFKKFS

Approximately 54 kDa, based on SDS-PAGE under reducing conditions.

≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of 10 mM Tris-HCl, 1 mM EDTA, 6% trehalose, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.