所有图片(1)
别名:
116-9e, 4-[1,1′-Biphenyl]-4-yl-3,4-dihydro-6-methyl-2-oxo-5-[(phenylmethoxy)carbonyl]-1(2H)-pyrimidinehexanoic acid
经验公式（希尔记法）:
C31H32N2O5
推荐产品
质量水平
检测方案
≥98% (HPLC)
形式
powder
颜色
white to off-white
溶解性
DMSO: >20 mg/mL
储存温度
2-8°C
SMILES字符串
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)
InChI key
GHFQWLNXJMUCGC-UHFFFAOYSA-N
应用
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.
生化/生理作用
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.
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.
警示用语：
Danger
危险声明
危险分类
Acute Tox. 3 Oral - Aquatic Acute 1 - Aquatic Chronic 1
储存分类代码
6.1C - Combustible, acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
新产品
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
我们的科学家团队拥有各种研究领域经验，包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系技术服务部门