Analytical Data
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Gene name
D2HGDH
- Application
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Alternative Names
D2HGDH；D2HGD；D-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
Q8N465
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Expression Region
14-521aa
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AA Sequence
LRGAPGAAGSWGRPVGPLARRGCCSAPGTPEVPLTRERYPVRRLPFSTVSKQDLAAFERIVPGGVVTDPEALQAPNVDWLRTLRGCSKVLLRPRTSEEVSHILRHCHERNLAVNPQGGNTGMVGGSVPVFDEIILSTARMNRVLSFHSVSGILVCQAGCVLEELSRYVEERDFIMPLDLGAKGSCHIGGNVATNAGGLRFLRYGSLHGTVLGLEVVLADGTVLDCLTSLRKDNTGYDLKQLFIGSEGTLGIITTVSILCPPKPRAVNVAFLGCPGFAEVLQTFSTCKGMLGEILSAFEFMDAVCMQLVGRHLHLASPVQESPFYVLIETSGSNAGHDAEKLGHFLEHALGSGLVTDGTMATDQRKVKMLWALRERITEALSRDGYVYKYDLSLPVERLYDIVTDLRARLGPHAKHVVGYGHLGDGNLHLNVTAEAFSPSLLAALEPHVYEWTAGQQGSVSAEHGVGFRKRDVLGYSKPPGALQLMQQLKALLDPKGILNPYKTLPSQA
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Molecular Weight
70.8kDa
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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
D2HGDH (D-2-hydroxyglutarate dehydrogenase) is an important enzyme involved in the metabolic pathway of D-2-hydroxyglutarate (D-2-HG), which is an oncometabolite associated with several types of cancer, particularly gliomas. The accumulation of D-2-HG is primarily due to mutations in the IDH1 or IDH2 genes, leading to disrupted metabolic processes and altered cellular functions. Understanding the role of D2HGDH in the degradation of D-2-HG has significant implications for cancer therapy, as its activity can influence tumor progression and response to treatment. Consequently, there is a growing interest in studying D2HGDH as a potential therapeutic target. Recombinant D2HGDH protein is being developed for various applications, including drug screening, understanding the enzyme's kinetics and structure, and elucidating its role in cellular metabolism. By producing and characterizing this recombinant protein, researchers aim to explore its enzymatic properties, regulation, and potential interactions with inhibitors, which could lead to novel strategies for managing IDH-mutant tumors. Furthermore, investigating D2HGDH can provide insights into the metabolic rewiring of cancer cells and their adaptation to the tumor microenvironment, thus unveiling new avenues for targeted therapies. Overall, the study of recombinant D2HGDH represents a significant step forward in cancer research, emphasizing the importance of metabolic enzymes in tumor biology and paving the way for innovative cancer treatments.
