Analytical Data
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Gene name
L2HGDH
- Application
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Alternative Names
L2HGDH；C14orf160；L-2-hydroxyglutarate dehydrogenase. mitochondrial
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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
Q9H9P8
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Expression Region
52-463aa
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AA Sequence
VIVGGGIVGLASARALILRHPSLSIGVLEKEKDLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALLYEYCQQKGISYKQCGKLIVAVEQEEIPRLQALYEKGLQNGVPGLRLIQQEDIKKKEPYCRGLMAIDCPHTGIVDYRQVALSFAQDFQEAGGSVLTNFEVKGIEMAKESPSRSIDGMQYPIVIKNTKGEEIRCQYVVTCAGLYSDRISELSGCTPDPRIVPFRGDYLLLKPEKCYLVKGNIYPVPDSRFPFLGVHFTPRMDGSIWLGPNAVLAFKREGYRPFDFSATDVMDIIINSGLIKLASQNFSYGVTEMYKACFLGATVKYLQKFIPEITISDILRGPAGVRAQALDRDGNLVEDFVFDAGVGDIGNRILHVRNAPSPAATSSIAISGMIADEVQQRFEL
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Molecular Weight
61.3kDa
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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
L2HGDH (L-2-hydroxyglutarate dehydrogenase) is an essential enzyme involved in the metabolism of L-2-hydroxyglutarate (2-HG), a metabolite that has gained attention due to its association with various neurological disorders and certain types of cancers, particularly gliomas. Mutations in the L2HGDH gene can lead to a rare metabolic disorder known as L-2-hydroxyglutaric aciduria, which is characterized by elevated levels of 2-HG in the body, resulting in neurological symptoms and developmental issues. Research into the recombinant production of L2HGDH protein seeks to elucidate its biochemical properties, functional mechanisms, and potential therapeutic applications. By utilizing recombinant DNA technology, scientists can produce large quantities of this enzyme, allowing for detailed studies on its enzymatic activity, structure-function relationships, and interactions with substrates and inhibitors. Furthermore, understanding the role of L2HGDH in cellular metabolism and its implications in disease processes could pave the way for innovative diagnostic and treatment strategies for conditions associated with dysregulation of 2-HG levels. The quest for effective therapies targeting L2HGDH and the pathways it influences has become increasingly relevant in precision medicine, as the knockdown of this enzyme has shown potential in altering metabolic profiles that drive tumorigenesis. Therefore, the study of recombinant L2HGDH not only contributes to basic biological knowledge but also has significant implications for the development of novel therapeutic approaches in oncology and neurology.
