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E1036

Sigma-Aldrich

116-9e

≥98% (HPLC), powder

Synonyme(s) :

116-9e, 4-[1,1′-Biphenyl]-4-yl-3,4-dihydro-6-methyl-2-oxo-5-[(phenylmethoxy)carbonyl]-1(2H)-pyrimidinehexanoic acid

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About This Item

Formule empirique (notation de Hill):
C31H32N2O5
Numéro CAS:
831217-43-7
Poids moléculaire :
512.60
Numéro MDL:
MFCD18632539
Code UNSPSC :
12352200
ID de substance PubChem :
329798875
Nomenclature NACRES :
NA.77

Niveau de qualité

100

Pureté

≥98% (HPLC)

Forme

powder

Couleur

white to off-white

Solubilité

DMSO: >20 mg/mL

Température de stockage

2-8°C

Chaîne SMILES 

CC1=C(C(NC(=O)N1CCCCCC(O)=O)c2ccc(cc2)-c3ccccc3)C(=O)OCc4ccccc4

InChI

1S/C31H32N2O5/c1-22-28(30(36)38-21-23-11-5-2-6-12-23)29(32-31(37)33(22)20-10-4-9-15-27(34)35)26-18-16-25(17-19-26)24-13-7-3-8-14-24/h2-3,5-8,11-14,16-19,29H,4,9-10,15,20-21H2,1H3,(H,32,37)(H,34,35)

Clé InChI

GHFQWLNXJMUCGC-UHFFFAOYSA-N

Application

116-9e has been used as an inhibitor of heat shock protein 70 (Hsp70) co-chaperone HDJ2 (human Ydj1/DNAJA1) to study the influence of HDJ2 on the regulation of ribonucleotide reductase (RNR) activity in HEK293 cells. It has also been used as an Hsp70 inhibitor to study the effect of Hsp70 chaperone on b5‐ops glycosylation in the side populations (SP) HeLa cells.

Actions biochimiques/physiologiques

116-9e is a blocker of Hsp40-Hsp70 binding thereby inhibiting the chaperone activity of Hsp70-Hsp40. The Hsp40 family of co–chaperones binds to Hsp70 through a conserved J–domain. It is believed that 116-9e inhibits chaperone functions by preventing Hsp70–Hsp40 complex assembly.

The same compound by a different name, MAL2-11B, has been found to inhibit the activity of a viral J-domain protein, large tumor antigen (TAg). MAL2-11B inhibited both TAg′s endogenous ATPase activity and the TAg-mediated activation of Hsp70.
116-9e is a dihhydropyrimidine compound.

Pictogrammes

Skull and crossbonesEnvironment
GHS06,GHS09

Mention d'avertissement

Danger

Mentions de danger

H301 - H410

Conseils de prudence

P273 - P301 + P310 + P330

Classification des risques

Acute Tox. 3 Oral - Aquatic Acute 1 - Aquatic Chronic 1

Code de la classe de stockage

6.1C - Combustible, acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Bruna Figueiredo Costa et al.
Traffic (Copenhagen, Denmark), 19(3), 182-197 (2018-01-24)
Tail-anchored (TA) proteins insert into their target organelles by incompletely elucidated posttranslational pathways. Some TA proteins spontaneously insert into protein-free liposomes, yet target a specific organelle in vivo. Two spontaneously inserting cytochrome b5 forms, b5-ER and b5-RR, which differ only
Isaac T Sluder et al.
PLoS genetics, 14(11), e1007462-e1007462 (2018-11-20)
Hsp70 is a well-conserved molecular chaperone involved in the folding, stabilization, and eventual degradation of many "client" proteins. Hsp70 is regulated by a suite of co-chaperone molecules that assist in Hsp70-client interaction and stimulate the intrinsic ATPase activity of Hsp70.
Erina Matsuoka et al.
Functional plant biology : FPB (2019-06-21)
The heat shock protein 90 (HSP90) inhibitor, geldanamycin, is a chemical inducer of the heat shock response (HSR) in Arabidopsis. Geldanamycin is thought to activate the heat shock signal by dissociating the HSP90-heat shock factor (HSF) complex. Recent studies have

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