Analytical Data
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Gene name
ldh1
- Application
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Alternative Names
ldh1; l-ldhL; ldh; ldhL; ldhL1; lp_0537L-lactate dehydrogenase 1; L-LDH 1; EC 1.1.1.27
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Species
Lactobacillus plantarum
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P56512
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Expression Region
1-320aa
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Molecular Weight
61.2 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
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Protein Description
Lactate dehydrogenase (LDH) is a crucial enzyme involved in the anaerobic metabolism of glucose, converting pyruvate to lactate while regenerating NAD+ essential for glycolysis. LDH exists in multiple isoforms, with LDH-1 primarily found in the heart, brain, and red blood cells, playing a vital role in energy production and metabolic regulation. Research on recombinant LDH-1 has gained traction due to its potential applications in biomedical fields, particularly in understanding cardiac metabolism, ischemic injury, and cancer metabolism, where altered lactate production significantly affects tumor growth and proliferation. The expression of LDH-1 in various tissues can serve as a biomarker for different diseases, including myocardial infarction and certain cancers, making the study of this enzyme not only relevant for metabolic insights but also for clinical diagnostics. Advances in molecular biology techniques have facilitated the production of recombinant LDH-1, allowing for detailed studies of its structure, function, and interaction with other metabolic pathways. By examining LDH-1’s role in cellular metabolism and its potential therapeutic targets, researchers aim to enhance our understanding of metabolic diseases, develop novel diagnostic tools, and explore avenues for targeted therapies that could modulate lactate levels in pathological conditions. Thus, the exploration of recombinant LDH-1 has important implications for both fundamental research and clinical applications.
