Recombinant Mouse Prolyl endopeptidase/PREP Protein (His Tag) | PKSM040755

Recombinant Mouse Prolyl endopeptidase/PREP Protein (His Tag) | PKSM040755 | Gentaur US, UK & Europe Disrtribition

Synonyms: AI047692;AI450383;D10Wsu136e;PEP;Pop

Active Protein: N/A

Activity: A DNA sequence encoding the mature form of mouse PREP (Q9QUR6) (Leu2-Gln710) was expressed, with a polyhistidine tag at the N-terminus.

Protein Construction: A DNA sequence encoding the mature form of mouse PREP (Q9QUR6) (Leu2-Gln710) was expressed, with a polyhistidine tag at the N-terminus.

Fusion Tag: N-His

Species: Mouse

Expressed Host: Baculovirus-Insect Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

Stability and 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.

Molecular Mass: 82.9 kDa

Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% glycerol, 3mM DTT

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.

Research Area: N/A