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Human PNLIP Protein (His Tag)

PL,PNLIPD,PTL

Catalog Number P13564-H08H
Organism Species Human
Host Human Cells
Synonyms PL,PNLIPD,PTL
Molecular Weight The recombinant human PNLIP consists of 460 amino acids and predicts a molecular mass of 51 KDa. It migrates as an approximately 51 KDa band in SDS-PAGE under reducing conditions.
predicted N Lys 17
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human PNLIP (P16233) (Met1-Cys465) was expressed with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area Cancer |Signal transduction |Metabolism |Pathways and Processes |Metabolic signaling pathways |Lipid and lipoprotein metabolism |
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background PNLIP is an enzyme which belongs to the lipase family. Secreted from the pancreas, PNLIP is the primary lipase that hydrolyzes dietary fat molecules in the human digestive system, converting triglyceride substrates found in ingested oils to monoglycerides and free fatty acids. Bile salts secreted from the liver and stored in gallbladder are released into the duodenum where they coat and emulsify large fat droplets into smaller droplets, thus increasing the overall surface area of the fat, which allows the lipase to break apart the fat more effectively. The resulting monomers (2 free fatty acids and one 2-monoacylglycerol) are then moved by way of peristalsis along the small intestine to be absorbed into the lymphatic system by a specialized vessel called a lacteal.
Reference
  • Hegele RA, et al. (2001) Polymorphisms in PNLIP, encoding pancreatic lipase, and associations with metabolic traits. J Hum Genet. 46(6):320-4.
  • Thomas A, et al. (2005) Role of the lid hydrophobicity pattern in pancreatic lipase activity. J Biol Chem. 280(48):40074-83.
  • Colin DY, et al. (2008) Exploring the active site cavity of human pancreatic lipase. Biochem Biophys Res Commun. 370(3):394-8.