Analytical Data
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Gene name
Lpl
- Application
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Alternative Names
Lpl；LIPD；LipoProtein lipase
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Species
Mouse
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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
P11152
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Expression Region
28-474aa
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AA Sequence
ADAGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSG
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Molecular Weight
55.3 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
Related Products
Protein Description
Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism, primarily responsible for hydrolyzing triglycerides in lipoproteins into free fatty acids and glycerol, which can then be taken up by tissues for energy production or storage. Research into LPL has gained significant attention due to its vital role in maintaining lipid homeostasis and its implications in various metabolic disorders, including obesity, diabetes, and cardiovascular diseases. The understanding of LPL's function and regulatory mechanisms has been enhanced through studies involving its recombinant protein. By expressing LPL as a recombinant protein in suitable host systems, researchers can obtain large quantities of the enzyme for detailed biochemical characterization, kinetic studies, and structural analyses. This work not only facilitates the exploration of LPL's interactions with different lipoproteins and inhibitors but also aids in the development of therapeutic strategies targeting lipid metabolism disorders. Moreover, recombinant LPL can be utilized in the study of gene therapy approaches for inherited forms of hyperlipoproteinemia and other LPL-related diseases. As our understanding of LPL expands, it may lead to novel interventions that can better manage or treat metabolic diseases associated with lipid dysregulation, underscoring the importance of ongoing research in this area.
