Prolyl Endopeptidase/PREP Protein, Mouse (sf9, His)

The prolyl endopeptidase (PREP) protein is an enzyme capable of cleaving peptide bonds at the C-terminus of prolyl residues within peptides, particularly peptides up to about 30 amino acids in length.This enzymatic activity suggests a role for PREP in selective processing of peptides, particularly toward proline-containing substrates.Prolyl Endopeptidase/PREP Protein, Mouse (sf9, His) is the recombinant mouse-derived Prolyl Endopeptidase/PREP protein, expressed by Sf9 insect cells , with N-His labeled tag.

Prolyl Endopeptidase (PREP) is an enzyme that cleaves peptide bonds on the C-terminal side of prolyl residues within peptides, particularly those of shorter lengths, up to approximately 30 amino acids. This specificity for prolyl residues highlights PREP's role in the selective hydrolysis of peptide bonds in specific substrates. The enzyme's activity suggests its involvement in the regulation of peptides containing proline, which can be significant in various cellular processes. Although further research is required to fully elucidate its physiological functions, the identified substrate specificity positions PREP as a key player in the processing and modulation of proline-containing peptides (

Measured by its ability to convert 50 μM substrate benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin (Z-GP-AMC) to Z-Gly-Pro and 7-amino-4-methylcoumarin (AMC) that incubate in kinetic mode for 5 minutes. The specific activity is 21105.10 pmol/min/µg.

Mouse

Sf9 insect cells

N-His

Q9QUR6 (L2-Q710)

19072  [NCBI]

Partial

LSFQYPDVYRDETSVQEYHGHKICDPYSWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLSIWEGCDPVNRLWYCDLQQEPNGITGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNRNSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLHDVKNILQLHDLTTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTKEELEPMVFREVTVKGIDAADYQTIQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKFTIGHAWTTDYGCSDTKQHFEWLLKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNIEWIQ

79-83 kDa

≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of 20 mM Tris, 500 mM NaCl, pH 7.4, 10% Glycerol, 3 mM DTT, 5% trehalose, 5% mannitol and 0.01% Tween 80.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.