Analytical Data
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Gene name
LIPC
- Application
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Alternative Names
LIPC；HTGL；Hepatic triacylglycerol lipase
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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
P11150
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Expression Region
1-499aa
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AA Sequence
MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQGCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLVDWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAYPCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQFKIQFINQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKWENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQEKIFVKCEIKSKTSKRKIR
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Molecular Weight
55.9 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
LIPC, or hepatic lipase, is an important enzyme involved in lipid metabolism, specifically in the hydrolysis of triglycerides and phospholipids in lipoproteins. It plays a critical role in modulating lipid profile and cholesterol metabolism, making it a significant factor in cardiovascular health. The study of LIPC’s structure and function has gained interest due to its association with various metabolic disorders, including dyslipidemia, obesity, and cardiovascular diseases. The recombinant expression of LIPC allows researchers to investigate its enzymatic activity, regulatory mechanisms, and interaction with lipoproteins more effectively. Furthermore, understanding the biological role of LIPC can inform potential therapeutic strategies for treating lipid-related diseases. Scientists have made progress in producing recombinant LIPC using various expression systems, including bacteria and mammalian cells, enhancing the yield and activity of this enzyme. Studies employing LIPC recombinant proteins provide valuable insights into its catalytic function, substrate specificity, and implications in lipid metabolism, contributing to the growing body of knowledge in metabolic research and potential clinical applications.
