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Recombinant Mouse Prolyl endopeptidase/PREP Protein (His Tag)

SKU: PKSM040755-50

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Recombinant Mouse Prolyl endopeptidase/PREP Protein (His Tag)

 

SKU # PKSM040755
Expression Host Baculovirus-Insect Cells

 

 

Description

Synonyms AI047692, AI450383, D10Wsu136e, PEP, Pop
Species Mouse
Expression Host Baculovirus-Insect Cells
Sequence Leu2-Gln710
Accession Q9QUR6
Calculated Molecular Weight 82.9 kDa
Observed Molecular Weight 79-83 kDa
Tag N-His
Bio-activity Not validated for activity
  

 

Properties

Purity > 95 % as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method.
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% glycerol, 3mM DTT
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution Please refer to the printed manual for detailed information.



Background

Prolyl endopeptidase, also known as PREP, belongs to a distinct class of serine peptidases. It is a large cytosolic enzyme which was first described in the cytosol of rabbit brain as an oligopeptidase. Prolyl endopeptidase degrades the nonapeptide bradykinin at the Pro-Phe bond. It is involved in the maturation and degradation of peptide hormones and neuropeptides such as alpha-melanocyte-stimulating hormone, luteinizing hormone-releasing hormone (LH-RH), thyrotropin-releasing hormone, angiotensin, neurotensin, oxytocin, substance P and vasopressin. Prolyl endopeptidase's activity is confined to action on oligopeptides of less than 10 kD and it has an absolute requirement for the trans-configuration of the peptide bond preceding proline. It cleaves peptide bonds at the C-terminal side of proline residues.