Analytical Data
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Gene name
LPD
- Application
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Alternative Names
ACSBG1; BG1; BGM; GR-LACS; hBG1; hsBG; Bubblegum; Very Long-Chain Acyl-CoA Synthetase; Acyl Coenzyme A Synthetase Bubblegum Family, Member 1
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99PU5
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Expression Region
Met1~Asn271
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Molecular Weight
44kDa
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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
LPD (Lipoprotein Lipase-Related Protein) is a member of the lipase gene family that plays a crucial role in lipid metabolism and energy homeostasis. Understanding the function of LPD and its related proteins has garnered significant interest due to their potential implications in metabolic disorders, cardiovascular diseases, and obesity. Research into the recombinant production of LPD proteins has become increasingly important, as these proteins can serve as valuable tools for studying lipid metabolism mechanistically and developing therapeutic interventions. Traditional methods for protein purification often fall short in terms of yield and activity, prompting researchers to explore recombinant DNA technology to express LPD proteins in various host systems. Such techniques not only enhance the quantity and quality of the proteins produced but also allow for the introduction of specific post-translational modifications crucial for their functional activity. Moreover, recombinant LPD proteins provide a basis for structural analyses, enabling researchers to investigate functional domains and interaction mechanisms critical to lipid processing. Over the years, studies have elucidated the role of LPD in lipoprotein metabolism, unveiling its interactions with other lipid-modifying enzymes and cellular components. As the field of metabolic research continues to evolve, recombinant LPD proteins are expected to pave the way for novel insights into metabolic pathways and potential therapeutic targets for diseases associated with lipid dysregulation.
