OGDH Antibody [F21L21] Datasheet

Biological Description

Specificity	OGDH Antibody [F21L21] detects endogenous levels of total OGDH protein.
Background	OGDH serves as the E1 subunit of the 2-oxoglutarate dehydrogenase multienzyme complex within the tricarboxylic acid cycle in eukaryotic mitochondria. The complex assembles with dihydrolipoamide S-succinyltransferase and dihydrolipoamide dehydrogenase to decarboxylate 2-oxoglutarate into succinyl-CoA alongside CO2 release and NADH generation. Calcium ions bind to specific sites on OGDH, including regions like D114ADLD and E139SDLD equivalents, lowering the Km for 2-oxoglutarate to enhance substrate affinity under physiological concentrations. ADP activates the complex by decreasing substrate Km, while ATP and NADH exert inhibitory effects by elevating Km values and shifting NADH sensitivity thresholds. These allosteric modulations integrate OGDH activity with cellular energy status, adenine nucleotide ratios, and redox balance, channeling TCA flux toward oxidative phosphorylation or biosynthetic demands. The protein assembles into a cubic arrangement with cofactor-binding domains that swing relative to the core during catalysis, facilitating thiamine pyrophosphate-dependent decarboxylation, lipoamide swinging for acyl transfer, and NADH production. OGDH sustains NADH supply for electron transport while modulating reactive oxygen species from associated flavins. Dysregulation through mutations or inhibition impairs complex assembly and flux, linking to encephalopathy and neurodegenerative decline via mitochondrial dysfunction.

Specificity

OGDH Antibody [F21L21] detects endogenous levels of total OGDH protein.

Background

OGDH serves as the E1 subunit of the 2-oxoglutarate dehydrogenase multienzyme complex within the tricarboxylic acid cycle in eukaryotic mitochondria. The complex assembles with dihydrolipoamide S-succinyltransferase and dihydrolipoamide dehydrogenase to decarboxylate 2-oxoglutarate into succinyl-CoA alongside CO2 release and NADH generation. Calcium ions bind to specific sites on OGDH, including regions like D114ADLD and E139SDLD equivalents, lowering the Km for 2-oxoglutarate to enhance substrate affinity under physiological concentrations. ADP activates the complex by decreasing substrate Km, while ATP and NADH exert inhibitory effects by elevating Km values and shifting NADH sensitivity thresholds. These allosteric modulations integrate OGDH activity with cellular energy status, adenine nucleotide ratios, and redox balance, channeling TCA flux toward oxidative phosphorylation or biosynthetic demands. The protein assembles into a cubic arrangement with cofactor-binding domains that swing relative to the core during catalysis, facilitating thiamine pyrophosphate-dependent decarboxylation, lipoamide swinging for acyl transfer, and NADH production. OGDH sustains NADH supply for electron transport while modulating reactive oxygen species from associated flavins. Dysregulation through mutations or inhibition impairs complex assembly and flux, linking to encephalopathy and neurodegenerative decline via mitochondrial dysfunction.

Usage Information

Application

WB, IP

Dilution

WB	IP
1:1000	1:50

Reactivity

Human, Mouse, Rat, Monkey

Source

Rabbit Monoclonal Antibody

MW

110 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

References

https://pubmed.ncbi.nlm.nih.gov/28184304/
https://pubmed.ncbi.nlm.nih.gov/24495017/

Application Data

WB

Validated by Selleck

Lane 1: LNCap, Lane 2: Hela, Lane 3: DLD-1, Lane 4: MCF7