Y16
目录号 : GC34088
Y16 is an inhibitor of G-protein-coupled Rho GEFs. It blocks the binding of LARG, a DBL-family Rho guanine nucleotide exchange factor, with Rho (Kd = 80 nM).
Cas No.:429653-73-6
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Quality Control & SDS
- View current batch:
- Purity: >99.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Y16 is an inhibitor of G-protein-coupled Rho GEFs. It blocks the binding of LARG, a DBL-family Rho guanine nucleotide exchange factor, with Rho (Kd = 80 nM).
Y16 binds to the junction site of the DH-PH domains of LARG with a ?80 nM Kd and suppresses LARG catalyzed RhoA activation dose dependently. It is active in blocking the interaction of LARG and related G-protein–coupled Rho GEFs with RhoA without a detectable effect on other DBL family Rho GEFs, Rho effectors, or a RhoGAP. In cells, Y16 selectively inhibits serum-induced RhoA activity and RhoA-mediated signaling, effects that can be rescued by a constitutively active RhoA or ROCK mutant. By suppressing RhoA activity, Y16 inhibits mammary sphere formation of MCF7 breast cancer cells but does not affect the nontransforming MCF10A cells. Y16 works synergistically with Rhosin/G04, a Rho GTPase activation site inhibitor, in inhibiting LARG–RhoA interaction, RhoA activation, and RhoA-mediated signaling functions. Y16 effectively inhibits the growth, migration, and invasion activities of breast cancer cells[1].
[1] Xun Shang, et al. Proc Natl Acad Sci U S A. 2013, 110(8):3155-60. [2] Diviani D, et al. Cell Chem Biol. 2016, 23(9):1135-1146.
| Cas No. | 429653-73-6 | SDF | |
| Canonical SMILES | O=C(N1)/C(C(N1C2=CC=CC=C2)=O)=C\C3=CC(OCC4=CC(C)=CC=C4)=CC=C3 | ||
| 分子式 | C24H20N2O3 | 分子量 | 384.43 |
| 溶解度 | DMSO : 25 mg/mL (65.03 mM);Water : < 0.1 mg/mL (insoluble) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
||
| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
 |
1 mg | 5 mg | 10 mg |
| 1 mM | 2.6013 mL | 13.0063 mL | 26.0125 mL |
| 5 mM | 0.5203 mL | 2.6013 mL | 5.2025 mL |
| 10 mM | 0.2601 mL | 1.3006 mL | 2.6013 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Small chemical compounds Y16 and Rhosin can inhibit calcium sensitization pathway in vascular smooth muscle cells of spontaneously hypertensive rats
J Formos Med Assoc 2021 Oct;120(10):1863-1868.PMID:33893012DOI:10.1016/j.jfma.2021.03.031.
Background/purpose: The small-molecule compounds Y16 and Rhosin can inhibit the activation of leukemia-associated Rho guanine nucleotide exchange factor (LARG) and small G-protein RhoA, respectively, in breast cancer cells and inhibit their growth and migration. However, it remains unclear whether they have inhibitory effects on the vascular smooth muscle cells (VSMCs) of spontaneously hypertensive rats (SHRs). Methods: Primary cultured VSMCs from SHRs were treated with different concentrations of Y16 or Y16 plus Rhosin for 24 h, followed by 10-min stimulation with 10-7 M angiotensin II (Ang II). The cells were then harvested, and the total protein was extracted. The co-immunoprecipitation method, Western blot analysis, and MTT assay were performed to determine the LARG-RhoA interaction, the protein levels of RhoA and MYPT1, and cell viability, respectively. Results: Y16 dose-dependently inhibited the LARG-RhoA complex formation induced by Ang II. With 50 μM of Y16, the effect of inhibition was statistically significant. Y16 also reduced the formation of phospho-MYPT1 stimulated by Ang II. With 5 μM of Y16, the inhibitory effect was statistically significant. When 25 μM of Y16 and 25 μM of Rhosin were combined, the inhibitory effect on LARG-RhoA interaction was statistically significant. When Y16 and Rhosin were combined, a significantly reduced concentration could effectively inhibit MYPT1 phosphorylation (2.5 μM compared with 5 μM for Y16 alone). Conclusion: Treating SHR VSMCs with Y16 can suppress the activation of LARG, prevent LARG binding to RhoA, and decrease the phosphorylation of MYPT1, thus weakening the activation of the calcium (Ca2+) sensitization pathway in SHR VSMCs.
Bacillus subtilis Y16 and biogas slurry enhanced potassium to sodium ratio and physiology of sunflower (Helianthus annuus L.) to mitigate salt stress
Environ Sci Pollut Res Int 2021 Aug;28(29):38637-38647.PMID:33735413DOI:10.1007/s11356-021-13419-2.
Salinity harms crop productivity; thereby, the management of salt-affected soils is a prerequisite to obtaining optimum crop yields and achieving UN-SDGs. The application of bio-organic amendments is an eco-friendly and cost-effective technique for the management of salt-affected soils. Therefore, this study examined the effect of salt-tolerant Bacillus subtilis strain Y16 and biogas slurry (BGS) on growth, physiology, and yield of sunflower under salt-affected soil conditions. Three levels of soil salinity (original electrical conductivity (EC): 3 dS m-1; induced EC: 6 dS m-1 and 8 dS m-1) were evaluated against three levels of BGS (0 kg ha-1, 600 kg ha-1, and 800 kg ha-1) with and without bacterial inoculation. Soil salinity (EC = 8 dS m-1) significantly (P < 0.05) increased Na+ contents (86%), which significantly (P < 0.05) reduced growth (17-56%), physiology (39-53%), and yield (58%) of sunflower. However, the combined application of BGS and B. subtilis alleviated salt stress and significantly (P < 0.05) improved sunflower growth (11-179%), physiology (10-84%), and yield (106%). The correlation analysis showed the superiority of B. subtilis for inducing salt-stress tolerance in sunflower as compared to BGS through homeostasis of K+/Na+ ratio. The tolerance indices and heat map analysis revealed an increased salt-stress tolerance in sunflower by the synergistic application of BGS and B. subtilis at original (3 dS m-1) and induced (6 dS m-1) soil salinity. Based on the results, we conclude that the combined application of B. subtilis and BGS enhanced growth and yield of sunflower by improving physiological processes and adjustment of K+/Na+ ratio in shoot under moderate salt-stress soil conditions.
Trehalose supplementation enhanced the biocontrol efficiency of Sporidiobolus pararoseus Y16 through increased oxidative stress tolerance and altered transcriptome
Pest Manag Sci 2021 Oct;77(10):4425-4436.PMID:33987938DOI:10.1002/ps.6477.
Background: In the process of biological control, the antagonistic yeasts contend with various stresses that negatively influence yeasts' biocontrol efficiency. In the current study, we investigated the effect of trehalose supplementation on the biocontrol efficiency and oxidative stress tolerance of Sporidiobolus pararoseus Y16. Results: S. pararoseus Y16, an antagonistic yeast cultured in trehalose supplemented medium, exhibited better biocontrol efficiency against Penicillium expansum and Aspergillus tubingensis in table grapes. Trehalose-treated S. pararoseus Y16 cells showed good proliferation efficiency and oxidative stress tolerance than untreated cells. Increased β-1,3-glucanase, catalase, superoxide dismutase activity, and low protein carbonylation were observed in trehalose-amended S. pararoseus Y16 upon H2 O2 exposure. The RNA sequencing results indicated that trehalose significantly altered the transcriptome of S. pararoseus Y16. The GO, KEGG, and COG annotations revealed that the differentially regulated genes corresponded to the various biological process of the yeast. Conclusion: Our findings suggested that trehalose use could enhance the biocontrol efficiency and oxidative stress tolerance of S. pararoseus Y16. Trehalose supplementation altered the transcriptome of S. pararoseus Y16, particularly the genes that correspond to amino acid metabolism, nucleotide metabolism, and protein modification. Thereby the oxidative stress tolerance and biological control efficiency of S. pararoseus Y16 was enhanced by trehalose. © 2021 Society of Chemical Industry.
Ammonium removal by a novel oligotrophic Acinetobacter sp. Y16 capable of heterotrophic nitrification-aerobic denitrification at low temperature
Bioresour Technol 2013 Oct;146:44-50.PMID:23911816DOI:10.1016/j.biortech.2013.07.046.
Ammonium removal from source water is usually inhibited by insufficient carbon sources and low temperature in Northeastern China. A strain Y16 was isolated from oligotrophic niche and was identified as Acinetobacter sp. Y16. It demonstrated excellent capability for ammonium removal at 2 °C, and simultaneously produced nitrogen gas as the end product. About 66% of ammonium was removed after 36 h of incubation. Only trace accumulation of nitrate was observed during the process. The utilization of nitrite and nitrate as well as the existence of napA gene further proved the aerobic denitrification ability of strain Y16. Sodium acetate was the most favorable carbon source for ammonium oxidation by strain Y16. High rotation speed was beneficial for ammonium oxidation. Furthermore, strain Y16 could efficiently remove ammonium at low C/N ratio and low temperature conditions, which was advantageous for nitrogen removal from source water under cold temperatures.
Purification and characterization of a low-temperature hydroxylamine oxidase from heterotrophic nitrifier Acinetobacter sp. Y16
Biomed Environ Sci 2014 Jul;27(7):515-22.PMID:25073910DOI:10.3967/bes2014.004.
Objective: To purify a low-temperature hydroxylamine oxidase (HAO) from a heterotrophic nitrifying bacterium Acinetobacter sp. Y16 and investigate the enzyme property. Methods: A HAO was purified by an anion-exchange and gel-filtration chromatography from strain Y16. The purity and molecular mass were determined by RP-HPLC and SDS-PAGE. The HAO activity was detected by monitoring the reduction of potassium ferricyanide using hydroxylamine as substrate and ferricyanide as electron acceptor. The partial amino acid sequence was determined by mass spectrometry. Results: The low-temperature HAO with a molecular mass of 61 kDa was purified from strain Y16 by an anion-exchange and gel-filtration chromatography. The enzyme exhibited an ability to oxidize hydroxylamine in wide temperature range (4-40 °C) in vitro using hydroxylamine as substrate and ferricyanide as electron acceptor. It was stable in the temperature range of 4 to 15 °C and pH range of 6.0 to 8.5 with less than 30% change in its activity. The optimal temperature and pH were 15 °C and 7.5, respectively. Three peptides were determined by mass spectrometry which were shown to be not identical to other reported HAOs. Conclusion: This is the first study to purify a low-temperature HAO from a heterotrophic nitrifier Acinetobacter sp. It differs from other reported HAOs in molecular mass and enzyme properties. The findings of the present study have suggested that the strain Y16 passes through a hydroxylamine-oxidizing process catalyzed by a low-temperature HAO for ammonium removal.