Analytical Data
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Gene name
lldD
- Application
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Alternative Names
lldD;lctD;L-lactate dehydrogenase
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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
A8A670
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Expression Region
1-396aa
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AA Sequence
MIISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSLVQGLGKELPAALAPMAKGNAA
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Molecular Weight
46.7kDa
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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
The study of lldD recombinant protein is anchored in the understanding of metabolic pathways involved in the utilization of lactate as a carbon source by certain microorganisms. lldD, or lactate dehydrogenase, plays a pivotal role in converting L-lactate to pyruvate, thereby facilitating energy production and metabolic flexibility in diverse environments. This enzyme is particularly significant in prokaryotes, where it aids in the anaerobic metabolism of lactate, and has implications in biotechnological applications, including bioenergy production and fermentation processes. Research on recombinant lldD not only enhances the comprehension of microbial metabolism but also offers insights into how these pathways can be harnessed for industrial purposes. Advances in molecular cloning and protein expression technologies have enabled the production of large quantities of purified lldD, providing opportunities for in-depth studies of its biochemical properties and substrate specificity. Understanding the structure-function relationship of lldD could lead to novel applications in metabolic engineering, aimed at optimizing microbial strains for improved lactate utilization. Furthermore, investigating lldD and its variants can shed light on evolutionary adaptations in microbial communities, contributing to ecological studies related to carbon cycling and sustainable practices. Thus, the exploration of lldD recombinant protein is not only crucial for basic research but also holds potential for applied sciences, including agriculture, environmental management, and renewable energy.
