Human LPL Recombinant Protein (N-His)
- Catalog number: PH10644
- Availability: In Stock
$211.00
- Ex Tax: $211.00
- Description: Recombinant Human LPL Protein, N-His (PH10644) expressed in E. coli, spanning His55-Glu316. Purity: >90% by SDS-PAGE.
Highlights:
• His-Tagged — N-terminal 6×His tag for IMAC purification.
• E. coli Expression — High-yield, cost-effective production.
• High Purity — >90% purity verified by SDS-PAGE. - Form: Lyophilized
- Storage buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
- Purity: >90% as determined by SDS-PAGE.
- Applications: ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
- Endotoxin level: Please contact with the lab for this information.
- Expression system: E. coli
- Protein length: His55-Glu316
- Predicted molecular weight: 31.23 kDa
- Stability and Storage: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
- Reconstitution: Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
- Alternative Names: Phospholipase A1, LIPD, Lipoprotein lipase, LPL
- Species: Homo sapiens (Human)
- Shipping: In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
- Background: Lipoprotein lipase (LPL/LIPD) is a ~53 kDa protein. Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.
References:
1. Lutz, EP. et al. (2001) The Journal of clinical investigation 107, 1183-92. PMID: 11342582
2. Pingitore, P. et al. (2016) Journal of clinical lipidology 10, 816-823. PMID: 27578112
3. Weinstock, PH. et al. (1995) The Journal of clinical investigation 96, 2555-68. PMID: 8675619
4. McCoy, MG. et al. (2002) Journal of lipid research 43, 921-9. PMID: 12032167
5. Dugi, KA. et al. (1995) The Journal of biological chemistry 270, 25396-401. PMID: 7592706
6. Goulbourne, CN. et al. (2014) Cell metabolism 19, 849-60. PMID: 24726386
7. Allan, CM. et al. (2017) Journal of lipid research 58, 216-225. PMID: 27811232 - Note: For research use only.
Images
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SDS-PAGESDS-PAGE for Recombinant Human LPL Protein, N-His.
