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.
E1411
Proline Specific Endopeptidase from Flavobacterium sp.
lyophilized powder, ≥5.0 units/mg solid
Proline Specific Endopeptidase from Flavobacterium sp.
1 of 1 reviewers received a sample product or took part in a promotion
Synonym(s):
EndoProC, Endoprolylpeptidase, Endoproteinase Pro-C, PEPase, Prolyl Endopeptidase
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| Size/SKU | Availability | Price |
|---|---|---|
50 units | Please contact Customer Service for Availability | PLN 2,840.00 |
About This Item
NACRES:
NA.54
UNSPSC Code:
12352204
Specific activity:
≥5.0 units/mg solid
Biological source:
bacterial (Flavobacterium spp.)
PLN 2,840.00
Please contact Customer Service for Availability
biological source
bacterial (Flavobacterium spp.)
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 [1]. Prolyl endopeptidase (PEP) may be used as a drug target for neuropsychiatric diseases such as stress disorder, depression, and schizophrenia [1].
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 [1].
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
This Item | |||
|---|---|---|---|
| specific activity ≥5.0 units/mg solid | specific activity ≥1,000 units/mg solid | specific activity ≥30 units/mg protein | specific activity ≥2 AU/mg protein |
| biological source bacterial (Flavobacterium spp.) | biological source bacterial (LYSOBACTER SP. BACTERIA M497-1) | biological source - | biological source - |
| form lyophilized powder | form lyophilized powder | form lyophilized powder | form lyophilized |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| mol wt ~78 kDa | mol wt 27 kDa | mol wt 28.93 kDa | mol wt - |
| shipped in dry ice | shipped in dry ice | shipped in wet ice | shipped in wet ice |
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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