I am extremely dissatisfied with the Proline Specific Endopeptidase from Flavobacterium sp. Despite strictly following the enzyme activity assay instructions to cleave Cytochrome C at a concentration of 1 mg/ml in PBS, with pH adjustments tried at both 6.5 and 7.0, the results were utterly disappointing. I experimented with enzyme to substrate ratios of 1:20, 1:50, and 1:100, incubating each mixture at 37°C for over 20 hours. Despite these efforts, mass spectrometry analysis revealed absolutely no cleavage, indicating that the enzyme activity was non-existent. This product is completely ineffective, and I strongly advise against wasting time and resources on it.
Fortfahren mit
E1411
Proline Specific Endopeptidase from Flavobacterium sp.
lyophilized powder, ≥5.0 units/mg solid
1 of 1 reviewers received a sample product or took part in a promotion
Synonym(e):
EndoProC, Endoprolylpeptidase, Endoproteinase Pro-C, PEPase, Prolyl Endopeptidase
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| Größe/SKU | Verfügbarkeit | Preis |
|---|---|---|
50 units | Warenkorb auf Verfügbarkeit prüfen | € 544,00 |
Über diesen Artikel
NACRES:
NA.54
UNSPSC Code:
12352204
Specific activity:
≥5.0 units/mg solid
Biological source:
bacterial (Flavobacterium spp.)
€ 544,00
Warenkorb auf Verfügbarkeit prüfen
Technischer Dienst
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Unterstützung erhaltenbiological source
bacterial (Flavobacterium spp.)
Quality Segment
form
lyophilized powder
specific activity
≥5.0 units/mg solid
mol wt
~78 kDa
shipped in
dry ice
storage temp.
−20°C
Application
Proline specific endopeptidase is useful for the determination of amino acid sequences of peptides and proteins containing proline residues. Proline specific endopeptidases may be useful in cancer, neurology and diabetes research . Prolyl endopeptidase (PEP) may be used as a drug target for neuropsychiatric diseases such as stress disorder, depression, and schizophrenia .
Biochem/physiol Actions
An endopeptidase is a proteolytic peptidase that breaks peptide bonds of nonterminal amino acids. Product E1411 is specific for proline (Pro). The Prolyl endopeptidase (PEP) mechanism is thought to be an induced fit mechanism, where the native enzyme exists in a conformationally flexible opened state but is changed to a closed state upon substrate binding .
Physical form
White amorphous lyophilized powder
Other Notes
One unit causes the formation of one micromole of p-nitroaniline per minute under specific pH and temperature conditions.
1 of 1
Dieser Artikel | |||
|---|---|---|---|
| description lyophilized powder, ≥5.0 units/mg solid | description recombinant, expressed in E. coli | description lyophilized powder (with BSA as stabilizer) | description Lyophilized powder stabilized with approx. 25% (w/w) bovine serum albumin, ≥30 units/mg protein (enzyme + BSA) |
| biological source bacterial (Flavobacterium spp.) | biological source - | biological source bacterial (Flavobacterium heparinum) | biological source bacterial (Flavobacterium heparinum) |
| specific activity ≥5.0 units/mg solid | specific activity ≥10 unit/μg protein | specific activity - | specific activity ≥30 units/mg protein (enzyme + BSA) |
| form lyophilized powder | form solution | form lyophilized powder (with BSA as stabilizer) | form lyophilized powder |
| shipped in dry ice | shipped in dry ice | shipped in dry ice | shipped in - |
| storage temp. −20°C | storage temp. −70°C | storage temp. −20°C | storage temp. −20°C |
| mol wt ~78 kDa | mol wt 81.6 kDa | mol wt - | mol wt 70.8 kDa |
Lagerklasse
11 - Combustible Solids
Was ist los?
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
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