OGDH Antibody [F21L21] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Monkey

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

Usage Information

Dilution
WB1:1000 IP1:50

Application
WB, IP

Reactivity
Human, Mouse, Rat, Monkey

Source
Rabbit Monoclonal Antibody

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

Predicted MW
110 kDa

Datasheet & SDS

Biological Description

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

Clone
F21L21

Synonym(s)
2-oxoglutarate dehydrogenase, mitochondrial; Alpha-ketoglutarate dehydrogenase; OGDH

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.

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.

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

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%