Analytical Data
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Gene name
lgt
- Application
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Alternative Names
lgt；umpA；Phosphatidylglycerol--prolipoProtein diacylglyceryl transferase
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Species
E.coli
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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
Q9CHU9
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Expression Region
1-261aa
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AA Sequence
MNNLFPFLALNKIALQLGPLAIHWYAIFIVGGAALAVWLACKEAPKRNIKTDDIIDFVLFAFPLGIVGARLYYVIFQWSYYSQHPSQIIAMWDGGGAIYGSLIAGAIVLFVFSYYRMIHPLDLLDITIPGVFLAQAMGRWGNFVNQEAYGKIVSNLDWLPAFIRNQMFIDGHYRMPTFLFESIGTLSGFILVMVFRHRIKGLKRGDIFSFYLVWYGAVRFIVEGMRTDSLMLGPARVSQWLSVLLVIVGLVLFIYRRMKKN
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Molecular Weight
29.7 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 metabolic pathway of glycolysis, facilitating the conversion of lactate to pyruvate. Its activity plays a significant role in various physiological and pathological processes, including cellular energy production and the response to hypoxia. The study of recombinantly expressed LDH (rLDH) has gained traction due to its potential applications in both basic research and clinical settings. With advancements in molecular biology techniques, researchers can now produce rLDH in heterologous systems, allowing for large-scale purification and characterization. Investigating rLDH not only aids in understanding its kinetic properties and regulatory mechanisms but also provides insights into its involvement in diseases such as cancer, where altered lactate metabolism is a hallmark. Moreover, rLDH can serve as an important biomarker for diagnostic purposes or as a therapeutic target, highlighting its relevance in drug development. Progress in structural biology, coupled with computational modeling, has further enhanced our knowledge of LDH's structural dynamics and interactions. Thus, the research surrounding rLDH continues to evolve, aiming to leverage its unique properties for innovative applications in biotechnology and medicine.
