Analytical Data
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Gene name
OGDH
- Application
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Alternative Names
OGDH；2-oxoglutarate dehydrogenase complex component E1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q02218
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Expression Region
41-427aa
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AA Sequence
SAPVAAEPFLSGTSSNYVEEMYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNVDKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDESDLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFETPGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSENGVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINRVTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVRPRERRARQIVKAPCSSMEFRSPT
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Molecular Weight
59.1kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
The study of OGDH (Oxoglutarate Dehydrogenase) recombinant protein has gained significant interest in the field of biochemistry and metabolic research due to its central role in cellular metabolism. OGDH is a key enzyme in the tricarboxylic acid (TCA) cycle, where it catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA, generating NADH in the process. This reaction not only contributes to ATP production but also ties into various metabolic pathways, influencing the synthesis of amino acids and neurotransmitters. Dysregulation of OGDH has been implicated in several diseases, including neurodegenerative conditions and cancer, making it a crucial target for therapeutic interventions. The recombinant production of OGDH facilitates in-depth studies on its structural and functional characteristics, enabling researchers to explore its mechanisms of action and regulation. Additionally, these studies provide insights into the enzyme's role in metabolic disorders and may lead to the development of novel strategies for disease treatment. Advances in protein engineering and expression systems have streamlined the generation of high-purity recombinant OGDH, allowing for comprehensive biochemical and biophysical analyses. Understanding the dynamics of OGDH at a molecular level is essential for uncovering its biological significance and potential as a biomarker or therapeutic target. Thus, the research on OGDH recombinant protein not only contributes to the fundamental understanding of metabolic processes but also holds promising implications for medical science and biotechnology.
