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SML0205

Sigma-Aldrich

Z-Pro-prolinal

≥98% (HPLC)

Sinonimo/i:

Cbz-Pro-Prolinal, N-Benzyloxycarbonyl-L-prolyl-L-prolinal, Phenylmethyl (2S)-2-[(2S)-2-formylpyrrolidine-1-carbonyl]pyrrolidine-1-carboxylate, Z-Pro-Pro-CHO, Z-PP-CHO, Z-pro-pro-CHO, Z-prolyl-prolinal, ZPP

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5 MG
107,00 €
25 MG
415,00 €

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5 MG
107,00 €
25 MG
415,00 €

About This Item

Formula empirica (notazione di Hill):
C18H22N2O4
Numero CAS:
Peso molecolare:
330.38
Codice UNSPSC:
12352209
NACRES:
NA.77

107,00 €


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Livello qualitativo

Saggio

≥98% (HPLC)

Stato

powder

Condizioni di stoccaggio

desiccated

Colore

white to tan

Solubilità

DMSO: ≥10 mg/mL

Temperatura di conservazione

−20°C

Stringa SMILE

N2([C@@H](CCC2)C(=O)N3[C@@H](CCC3)C=O)C(=O)OCc1ccccc1

InChI

1S/C18H22N2O4/c21-12-15-8-4-10-19(15)17(22)16-9-5-11-20(16)18(23)24-13-14-6-2-1-3-7-14/h1-3,6-7,12,15-16H,4-5,8-11,13H2/t15-,16-/m0/s1
ORZXYSPOAVJYRU-HOTGVXAUSA-N

Categorie correlate

Applicazioni

Z-Pro-prolinal was used to inhibit activation of rekallikrein in Prolylcarboxypeptidase assay in HUVECs.[1] ZPP was also used in assays to identify enzymes important in the processing of angiotensin peptides in human glomerular endothelial cells.[2]

Azioni biochim/fisiol

Z-Pro-prolinal is a potent selective inhibitor of prolyl oligopeptidase (POP), also known as prolyl endopeptidase (PEP or PE).
Z-Pro-prolinal is a potent, selective inhibitor of Prolyl oligopeptidase (POP), also known as prolyl endopeptidase (PEP or PE). Ki = 1 nM.

POP has been connected to memory and mood through regulation of the brain levels of its peptide substrates, which include AVP, substance P, neurotensin and TRH and is a potential target in cognitive function, memory, and neurodegenerative disorders such as amnesia, Alzheimer′s disease, and depression. POP has recently been reported to be involved in the release of the tetrapeptide acetyl-N-Ser-Asp-Lys-Pro (Ac-SDKP) from its precursor, 43-mer thymosin β4 (Tβ4). Ac-SDKP is involved in hemopoietic stem cell differentiation, is pro-angiogenic and antifibrogenic.

Pittogrammi

Exclamation mark

Avvertenze

Warning

Indicazioni di pericolo

Classi di pericolo

Acute Tox. 4 Oral - Eye Irrit. 2

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Aurélien F A Moumbock et al.
Archiv der Pharmazie, 356(1), e2200371-e2200371 (2022-11-01)
Host cell entry of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is facilitated via priming of its spike glycoprotein by the human transmembrane protease serine 2 (TMPRSS2). Although camostat and nafamostat are two highly potent covalent TMPRSS2 inhibitors, they nevertheless
Charles M Ensor et al.
bioRxiv : the preprint server for biology (2021-09-22)
Angiotensin converting enzyme 2 (ACE2) is an enzyme that limits activity of the renin-angiotensin system (RAS) and also serves as a receptor for the SARS-CoV-2 Spike (S) protein. Binding of S protein to ACE2 causes internalization which activates local RAS.
Mikhail Lebedin et al.
iScience, 27(3), 109330-109330 (2024-03-18)
Identifying immune modulators that impact neutralizing antibody responses against severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) is of great relevance. We postulated that high serum concentrations of soluble angiotensin-converting enzyme 2 (sACE2) might mask the spike and interfere with
Mikhail Lebedin et al.
European journal of immunology, 53(5), e2250210-e2250210 (2023-03-02)
Diverse autoantibodies were suggested to contribute to severe outcomes of COVID-19, but their functional implications are largely unclear. ACE2, the SARS-CoV-2 receptor and a key regulator of blood pressure, was described to be one of many targets of autoantibodies in
Juan Carlos Q Velez et al.
American journal of physiology. Renal physiology, 302(12), F1583-F1594 (2012-03-31)
The intraglomerular renin-angiotensin system (RAS) is linked to the pathogenesis of progressive glomerular diseases. Glomerular podocytes and mesangial cells play distinct roles in the metabolism of angiotensin (ANG) peptides. However, our understanding of the RAS enzymatic capacity of glomerular endothelial

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