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经验公式(希尔记法):
C16H28N4O2
化学文摘社编号:
分子量:
308.42
NACRES:
NA.77
PubChem Substance ID:
UNSPSC Code:
12352200
MDL number:
InChI
1S/C16H28N4O2/c1-12(2)9-16(22,10-13(3)4)14-11-17-20(18-14)15(21)19-7-5-6-8-19/h11-13,22H,5-10H2,1-4H3
SMILES string
CC(C)CC(O)(CC(C)C)c1cnn(n1)C(=O)N2CCCC2
InChI key
GXBVPGCIMCIASQ-UHFFFAOYSA-N
assay
≥98% (HPLC)
form
film
color
colorless
solubility
DMSO: >15 mg/mL
storage temp.
2-8°C
Quality Level
Biochem/physiol Actions
AA74-1 is an extremely potent and selective inhibitor of the serine hydrolase acyl-peptide hydrolase (APEH) with an IC50 of 5 nM in mouse T-cell proteomes. AA74-1 potently blocked the activity of its target serine hydrolase, APEH, in mice in vivo without significantly affecting other enzymes. The APEH inhibition caused accumulation of N-acetylated proteins and stimulated cellular proliferation in T cells.
The APEH gene is deleted in some cancers, in which it has been proposed to serve as a potential tumor suppressor, and is involved in the degradation of oligomeric amyloid-beta which could make it a new target for therapy aimed at reducing neurodegeneration in Alzheimer′s disease. AA74-1 is the first selective tool for studying APEH activity.
The APEH gene is deleted in some cancers, in which it has been proposed to serve as a potential tumor suppressor, and is involved in the degradation of oligomeric amyloid-beta which could make it a new target for therapy aimed at reducing neurodegeneration in Alzheimer′s disease. AA74-1 is the first selective tool for studying APEH activity.
AA74-1 is an extremely potent and selective inhibitor of the serine hydrolase acyl-peptide hydrolase (APEH).
存储类别
11 - Combustible Solids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Rubayet Elahi et al.
mSphere, 4(3) (2019-05-10)
The human malaria parasite Plasmodium falciparum causes disease as it replicates within the host's erythrocytes. We have found that an erythrocyte serine hydrolase, acylpeptide hydrolase (APEH), accumulates within developing asexual parasites. Internalization of APEH was associated with a proteolytic event
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