Analytical Data
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Gene name
LDHD
- Application
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Alternative Names
LDHD；Probable D-lactate 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
Q86WU2
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Expression Region
1-507aa
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AA Sequence
MARLLRSATWELFPWRGYCSQKAKGELCRDFVEALKAVVGGSHVSTAAVVREQHGRDESVHRCEPPDAVVWPQNVEQVSRLAALCYRQGVPIIPFGTGTGLEGGVCAVQGGVCVNLTHMDRILELNQEDFSVVVEPGVTRKALNAHLRDSGLWFPVDPGADASLCGMAATGASGTNAVRYGTMRDNVLNLEVVLPDGRLLHTAGRGRHFRFGFWPEIPHHTAWYSPCVSLGRRKSAAGYNLTGLFVGSEGTLGLITATTLRLHPAPEATVAATCAFPSVQAAVDSTVHILQAAVPVARIEFLDEVMMDACNRYSKLNCLVAPTLFLEFHGSQQALEEQLQRTEEIVQQNGASDFSWAKEAEERSRLWTARHNAWYAALATRPGCKGYSTDVCVPISRLPEIVVQTKEDLNASGLTGSIVGHVGDGNFHCILLVNPDDAEELGRVKAFAEQLGRRALALHGTCTGEHGIGMGKRQLLQEEVGAVGVETMRQLKAVLDPQGLMNPGKVL
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Molecular Weight
54.8 kDa
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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
Related Products
Protein Description
LDHD (L-lactate dehydrogenase) is an enzyme that plays a crucial role in cellular metabolism, primarily involved in the conversion of pyruvate to lactate in anaerobic conditions. The research background of LDHD recombinant protein encompasses its significance in various physiological and pathological processes, including cancer metabolism, exercise physiology, and metabolic disorders. Elevated levels of lactate are often associated with tumor hypoxia and glycolytic activity, marking LDHD as a potential biomarker for cancer progression. Furthermore, understanding LDHD function and regulation can provide insights into metabolic pathways that are altered in diseases. The production of recombinant LDHD allows for detailed studies of its enzymatic properties and regulatory mechanisms, facilitating the development of targeted therapies or diagnostic tools in clinical settings. By elucidating the structure and function of LDHD, researchers aim to uncover new therapeutic avenues in treating conditions characterized by abnormal lactate metabolism, ultimately contributing to improved patient outcomes.
