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E1411

Sigma-Aldrich

Proline Specific Endopeptidase from Flavobacterium sp.

lyophilized powder, ≥5.0 units/mg solid

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Synonym(s):
EndoProC, Endoprolylpeptidase, Endoproteinase Pro-C, PEPase, Prolyl Endopeptidase
NACRES:
NA.54

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

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This Item
A3547O9515P2308
vibrant-m

A3547

Achromopeptidase from bacteria

vibrant-m

O9515

Prolyl oligopeptidase

biological source

bacterial (Flavobacterium spp.)

biological source

-

biological source

-

biological source

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

400

form

lyophilized powder

form

lyophilized powder

form

solution

form

lyophilized powder

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

wet ice

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

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 .

Unit Definition

One unit causes the formation of one micromole of p-nitroaniline per minute under specific pH and temperature conditions.

Physical form

White amorphous lyophilized powder

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Min Li et al.
The Journal of biological chemistry, 285(28), 21487-21495 (2010-05-07)
Prolyl peptidases cleave proteins at proline residues and are of importance for cancer, neurological function, and type II diabetes. Prolyl endopeptidase (PEP) cleaves neuropeptides and is a drug target for neuropsychiatric diseases such as post-traumatic stress disorder, depression, and schizophrenia.

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