BPIQ-I
(Synonyms: PD 159121) 目录号 : GC41631
A potent EGFR inhibitor
Cas No.:174709-30-9
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
BPIQ-I is a quinazoline that inhibits the tyrosine kinase activity of the epidermal growth factor receptor (IC50 = 0.025 nM). It can inhibit the growth of SKOV3 and MDA-468 tumor cell lines with EC50 values of 6.5 and 30 µM, respectively.
| Cas No. | 174709-30-9 | SDF | |
| 别名 | PD 159121 | ||
| Canonical SMILES | BrC1=CC=CC(NC2=C(C=C(N=CN3C)C3=C4)C4=NC=N2)=C1 | ||
| 分子式 | C16H12BrN5 | 分子量 | 354.2 |
| 溶解度 | DMF: 20 mg/ml,DMSO: 30 mg/ml,DMSO:PBS (pH 7.2) (1:1): 0.5 mg/ml | 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。 |
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| 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 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 2.8233 mL | 14.1163 mL | 28.2326 mL |
| 5 mM | 0.5647 mL | 2.8233 mL | 5.6465 mL |
| 10 mM | 0.2823 mL | 1.4116 mL | 2.8233 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。
Delta-opioid receptors activate ERK/MAP kinase via integrin-stimulated receptor tyrosine kinases
Cell Signal 2008 Dec;20(12):2324-31.PMID:18804531DOI:10.1016/j.cellsig.2008.09.002.
Integrin-mediated cell adherence to extracellular matrix proteins results in stimulation of ERK1/2 activity, a mechanism involving focal adhesion tyrosine kinases (pp125FAK, Pyk-2) and epidermal growth factor receptors (EGFRs). G protein-coupled receptors (GPCRs) may also mediate ERK1/2 activation in an integrin-dependent manner, the underlying signaling mechanism of which still remains unclear. Here we demonstrate that the delta-opioid receptor (DOR), a typical GPCR, stimulates ERK1/2 activity in HEK293 cells via integrin-mediated transactivation of EGFR function. Inhibition of integrin signaling by RGDT peptides, cytochalasin, and by keeping the cells in suspension culture both blocked [D-Ala(2), D-Leu(5)]enkephalin (DADLE)- and etorphine-stimulated ERK1/2 activity. Integrin-dependent ERK1/2 activation does not involve FAK/Pyk-2, because over-expression of the FAK/Pyk-2 inhibitor SOCS-3 failed to attenuate DOR signaling. Exposure of the cells to the EGFR inhibitors AG1478 and BPIQ-I blocked DOR-mediated ERK1/2 activation. Because RGDT peptides also prevented DOR-mediated EGFR activation, the present findings indicate that in HEK293 cells DOR-stimulated ERK1/2 activity is mediated by integrin-stimulated EGFRs. Further studies with the phospholipase C (PLC) inhibitors U73122 and ET-18-OCH(3) revealed that opioid-stimulated integrin activation is sensitive to PLC. In contrast, integrin-mediated transactivation of EGFR function appears to be dependent on PKC-delta, as indicated by studies with rottlerin and siRNA knock-down. A similar ERK1/2 signaling pathway was observed for NG108-15 cells, a neuronal cell line endogenously expressing the DOR. In these cells, the nerve growth factor TrkA receptor replaces the EGFR in connecting DOR-activated integrins to the Ras/Raf/ERK1/2 pathway. Together, these data describe an alternative ERK1/2 signaling pathway in which the DOR transactivates the growth factor receptor associated mitogen-activated protein kinase cascade in an integrin-dependent manner.
Role of a tyrosine kinase in the CO2-induced stimulation of HCO3- reabsorption by rabbit S2 proximal tubules
Am J Physiol Renal Physiol 2006 Aug;291(2):F358-67.PMID:16705143DOI:10.1152/ajprenal.00520.2005.
A previous study demonstrated that proximal tubule cells regulate HCO(3)(-) reabsorption by sensing acute changes in basolateral CO(2) concentration, suggesting that there is some sort of CO(2) sensor at or near the basolateral membrane (Zhou Y, Zhao J, Bouyer P, and Boron WF Proc Natl Acad Sci USA 102: 3875-3880, 2005). Here, we hypothesized that an early element in the CO(2) signal-transduction cascade might be either a receptor tyrosine kinase (RTK) or a receptor-associated (or soluble) tyrosine kinase (sTK). In our experiments, we found, first, that basolateral 17.5 microM genistein, a broad-spectrum tyrosine kinase inhibitor, virtually eliminates the CO(2) sensitivity of HCO(3)(-) absorption rate (J(HCO(3))). Second, we found that neither basolateral 250 nM nor basolateral 2 microM PP2, a high-affinity inhibitor for the Src family that also inhibits the Bcr-Abl sTK as well as the Kit RTK, reduces the CO(2)-stimulated increase in J(HCO(3)). Third, we found that either basolateral 35 nM PD168393, a high-affinity inhibitor of RTKs in the erbB (i.e., EGF receptor) family, or basolateral 10 nM BPIQ-I, which blocks erbB RTKs by competing with ATP, eliminates the CO(2) sensitivity. In conclusion, the transduction of the CO(2) signal requires activation of a tyrosine kinase, perhaps an erbB. The possibilities include the following: 1) a TK is simply permissive for the effect of CO(2) on J(HCO(3)); 2) a CO(2) receptor activates an sTK, which would then raise J(HCO(3)); 3) a CO(2) receptor transactivates an RTK; and 4) the CO(2) receptor could itself be an RTK.