Recombinant Human Pancreatic Lipase/PNLIP HA-tag His-tag, CF

R&D Systems, part of Bio-Techne | Catalog # 11773-PL

R&D Systems, part of Bio-Techne
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11773-PL-050
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Key Product Details

Source

CHO

Accession #

P16233.1

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Pancreatic Lipase Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Pancreatic Lipase protein
Lys17-Cys465, with N-terminal HA (YPYDVPDYA) and 6-His tags

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Tyr

Predicted Molecular Mass

52 kDa

SDS-PAGE

50-55 kDa, under reducing conditions.

Activity

Measured by its ability to cleave a fluorogenic substrate, 4-Methylumbelliferyl oleate (4-MUO).
The specific activity is >750 pmol/min/μg, as measured under the described conditions.

Scientific Data Images for Recombinant Human Pancreatic Lipase/PNLIP HA-tag His-tag, CF

Recombinant Human Pancreatic Lipase/PNLIP HA-tag His-tag Enzyme Activity.

Recombinant Human Pancreatic Lipase/PNLIP HA-tag His-tag (Catalog # 11773-PL) is measured by its ability to cleave a fluorogenic substrate, 4-Methylumbelliferyl oleate (4-MUO).

Recombinant Human Pancreatic Lipase/PNLIP HA-tag His-tag SDS-PAGE.

2 μg/lane of Recombinant Human Pancreatic Lipase/PNLIP HA-tag His-tag (Catalog # 11773-PL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 50-55 kDa, under reducing conditions.

Formulation, Preparation and Storage

11773-PL
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Pancreatic Lipase

Recombinant human pancreatic triacylglycerol lipase or pancreatic lipase (PL), from the gene PNLIP, is a 449 residue mature, glycosylated, secreted serine hydrolase of a family of mammalian lipases. Mature PL/PNLIP contains a globular N-terminal core domain typical of a/b hydrolase-fold family members and a C-terminal domain that is connected via an amino acid extension and seven disulfide bonds (1, 2). The C-terminal domain binds the required cofactor procolipase via a salt bridge but does not alter the conformation of the core PL/PNLIP domain (2). The N-terminal core domain contains the catalytic triad active site and a lid domain that inhibits binding of substrate and requires conformational change for activity through adsorption at the interface of lipid micelles (2). PL/PNLIP is secreted from the pancreas and hydrolyzes dietary fat triacylglycerides at the two carbon site at high preference over cholesterol esters, phospholipids, and galactolipids (3) playing a key role in absorption of dietary fat in the small intestine (2). As PL/PNLIP is the primary enzyme responsible for the hydrolysis of the majority of dietary fats in the proximal small intestine (4), inhibition has been identified as an important target for the prevention and treatment of obesity-related disorders such as diabetes, dyslipidemia, nonalcoholic fatty liver disease and cardiovascular disease (4-7). With a few available PL/PNLIP inhibitors in use in the clinic to manage obesity and its related disorders, significant investigation and development of additional or alternative inhibitors for PL/PNLIP with fewer side effects is underway (2, 9, 10). Pancreatic enzyme replacement therapies that include PL/PNLIP have shown high therapeutic value for patients with exocrine pancreatic insufficiency (EPI), a deficiency of the pancreatic enzymes resulting in maldigestion and malabsorption caused by many diseases such as pancreatic adenocarcinoma and cystic fibrosis or by a rare disorder known as congenital pancreatic triglyceride lipase (9, 11, 12).  Finally, oral lipid-based delivery systems are prone to digestion by pancreatic lipase in the small intestine which can impact the integrity of these delivery systems and result in premature drug release into the gastrointestinal environment and exposure of the drug to alteration by proteases in the small intestine (13); development of strategies including inhibition of PL/PNLIP to control potential impacts to oral lipid-based drug delivery systems is  under investigation (13).

References

  1. Winkler, F.K. et. al. (1990) Nature 343:771. 
  2. Kumar, A. and S. Chauhan (2021) Life Sci. 271:119115. 
  3. Lim, S.Y. et. al. (2022) Am. J. Vet Res. 83:1.
  4. Yadav, N. and A.T. Paul (2024) Drug Discov. Today 29:103855.
  5. Chatzigeorgiou, A. et. al. (2014) Hepatology 60:1196.
  6. Higgins, V. et. al. (2020) J. Clin. Endocrinol. Metab. 105:1228.
  7. Lee, S.S. and S. Kang (2015) J. Phys. Ther. Sci. 27:1903.
  8. Lopez-Jimenez, F. et. al. (2022) Eur. J. Prev. Cardiol. 29:2218.
  9. Subramaniyan, V. and Y.U. Hanim (2025) Int. J.  Obes. 49:492. 
  10. Uuh Narvaez, J.J. et. al. (2025) Molecules 30:2392. 
  11. Szabo, A. et. al. (2015) Biochim. Biophys. Acta 1852:1372.
  12. Brennan, G.T. and M.W. Saif (2019) JOP 20:121. 
  13. Zupancic, O. et. al. (2023) J. Control Release 362:381.

Long Name

Pancreatic triacylglycerol lipase

Alternate Names

PNLIP, PTL

Entrez Gene IDs

5406 (Human)

Gene Symbol

PNLIP

UniProt

P16233.1

Additional Pancreatic Lipase Products

Product Documents for Recombinant Human Pancreatic Lipase/PNLIP HA-tag His-tag, CF

Product Datasheets

Certificate of Analysis

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Product Specific Notices for Recombinant Human Pancreatic Lipase/PNLIP HA-tag His-tag, CF

For research use only

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