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Human Recombinant Pancreatic Lipase-Related 1 (from Cells)
Human Recombinant Pancreatic Lipase-Related 1 (from Cells)
# de catalogue 75789-812
Fournisseur:  Prosci
Numéro CAS:  
Human Recombinant Pancreatic Lipase-Related 1 (from Cells)
# de catalogue 75789-812
Fournisseur:  Prosci
Numéro CAS:  
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Spécifications

  • Enzyme type:
    Recombinant
  • Source:
    Cells
  • Species:
    Human
  • Size:
    0.05 mg
  • Storage conditions:
    Lyophilized protein should be stored at –20 °C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4...7 °C for 2 - 7 days. Aliquots of reconstituted samples are stable at –20 °C for 3 months.
  • Endotoxin content:
    <0.1 ng/ug (1 IEU/ug) as determined by LAL test.
  • Enzyme name:
    Pancreatic Lipase-Related 1
  • Enzyme synonyms:
    Pancreatic Lipase-Related Protein 1, PL-RP1, PNLIPRP1, PLRP1
  • Purity:
    >95% as determined by reducing SDS-PAGE
  • Molecular weight:
    50.99 kD
  • Sequence:
    Lys18-Cys467
  • Formulation:
    Lyophilized from a 0.2 µm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4. Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 ug/ml. Dissolve the Lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
  • Tested applications:
    Bioassay
  • Cat. no.:
    75789-812
  • Supplier No.:
    91-568

Spécifications

A propos de cet article

Pancreatic Lipase-Related Protein 1 (PNLIPRP1) belongs to the Lipase family within the AB hydrolase superfamily

This recombinant protein can be used for biological assays. For research use only.

Fusion-Tag: C-6 His tag

PNLIPRP1 is a secreted protein and contains one PLAT domain. PNLIPRP1 is involved in lipid metabolic process, acting as a negative regulator of pancreatic lipase activity by competing with pancreatic lipase for colipase occupancy. PNLIPRP1 may play a role in inhibiting dietary triglyceride digestion, but it lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters.

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