General Information of Experiment

Probe Name Alkylaryl probe 1  Probe Info 
Probe concentration 1 mM
Criteria Quantification: Probe vs DMSO
Quantitative Method
SILAC
In Vivo Experiment Model Model Type Living cell
Derived Tissue Peripheral blood
Disease Model Normal
Model Name Human normal cells (HEK-293T)

Interaction Altas of This Experiment [1]

Enzyme
Click to Show/Hide to Show 24 Protein Related to This Bioclass
Target ID Target Name Binding Ratio
 LDTP03511  Flavin reductase (NADPH) (BLVRB) 20.0
 LDTP10888  Legumain (LGMN) 20.0
 LDTP02918  S-adenosylmethionine decarboxylase proenzyme (AMD1) 20.0
 LDTP15725  Secernin-2 (SCRN2) 20.0
 LDTP17022  Secernin-3 (SCRN3) 20.0
 LDTP07979  FAST kinase domain-containing protein 5, mitochondrial (FASTKD5) 18.0
 LDTP02008  Fructose-bisphosphate aldolase A (ALDOA) 16.0
 LDTP02386  Fructose-bisphosphate aldolase C (ALDOC) 16.0
 LDTP07092  Probable arginine--tRNA ligase, mitochondrial (RARS2) 16.0
 LDTP07110  Putative transferase CAF17, mitochondrial (IBA57) 14.0
 LDTP02198  Cathepsin D (CTSD) 13.0
 LDTP15988  Probable serine carboxypeptidase CPVL (CPVL) 13.0
 LDTP04232  4-trimethylaminobutyraldehyde dehydrogenase (ALDH9A1) 12.0
 LDTP08476  5'-3' exonuclease PLD3 (PLD3) 12.0
 LDTP02837  Beta-galactosidase (GLB1) 12.0
 LDTP18414  5'-nucleotidase domain-containing protein 2 (NT5DC2) 11.0
 LDTP02141  Alpha-galactosidase A (GLA) 11.0
 LDTP07763  Kynurenine--oxoglutarate transaminase 3 (KYAT3) 10.0
 LDTP05992  Bleomycin hydrolase (BLMH) 9.0
 LDTP02074  Aldehyde dehydrogenase, mitochondrial (ALDH2) 8.0
 LDTP11842  Inorganic pyrophosphatase 2, mitochondrial (PPA2) 7.0
 LDTP03560  Aldehyde dehydrogenase X, mitochondrial (ALDH1B1) 6.0
 LDTP11199  DCN1-like protein 5 (DCUN1D5) 6.0
 LDTP16032  Retinoid-inducible serine carboxypeptidase (SCPEP1) 5.0
Other
Click to Show/Hide to Show 2 Protein Related to This Bioclass
Target ID Target Name Binding Ratio
 LDTP00398  Insulin receptor substrate 4 (IRS4) 20.0
 LDTP06051  Kelch-like ECH-associated protein 1 (KEAP1) 17.0

References

1 Hydrazines as versatile chemical biology probes and drug-discovery tools for cofactor-dependent enzymes. bioRxiv, 2020-06.