Analytical Data
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Gene name
ldh
- Application
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Alternative Names
ldh；Ldh-1；Ldh1；L-lactate dehydrogenase A chain
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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
P00338
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Expression Region
2-332aa
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AA Sequence
ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF
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Molecular Weight
44.1 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 conversion of pyruvate to lactate in anaerobic metabolism, playing a significant role in cellular energy production. It exists in various isoforms, which are expressed differently across tissues, making LDH a valuable biomarker for various diseases, including cancer and cardiovascular disorders. The study of recombinant LDH proteins has gained importance due to advances in genetic engineering and biotechnology, allowing for the production of these enzymes in heterologous systems. This enables researchers to obtain large quantities of pure protein for functional studies, structural analysis, and drug development. The recombinant LDH can be used to explore its enzymatic mechanisms, regulatory pathways, and interactions with other biomolecules. Furthermore, due to its involvement in metabolic shifts, LDH is being investigated as a therapeutic target, with inhibitors showing promise in cancer treatment. The establishment of recombinant LDH production systems has also enhanced the understanding of enzyme kinetics and facilitated the design of LDH-based biosensors. Overall, the research on recombinant LDH proteins not only contributes to basic science but also holds potential for clinical applications, offering insights into disease mechanisms and leading to novel therapeutic strategies.
