BZ1
(Synonyms: BPTF inhibitor, BPTF-IN-BZ1) 目录号 : GC25183BZ1 (BPTF inhibitor, BPTF-IN-BZ1) is a pyridazinone-based BPTF (Bromodomain PHD Finger Transcription Factor) inhibitor with a high potency (Kd = 6.3 nM) and >350-fold selectivity over BET bromodomains.
Cas No.:2766623-38-3
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
BZ1 (BPTF inhibitor, BPTF-IN-BZ1) is a pyridazinone-based BPTF (Bromodomain PHD Finger Transcription Factor) inhibitor with a high potency (Kd = 6.3 nM) and >350-fold selectivity over BET bromodomains.
[1] Zahid H, et al. J Med Chem. 2021 Sep 23;64(18):13902-13917.
| Cas No. | 2766623-38-3 | SDF | Download SDF |
| 别名 | BPTF inhibitor, BPTF-IN-BZ1 | ||
| 分子式 | C13H15ClN4O | 分子量 | 278.74 |
| 溶解度 | DMSO: 56 mg/mL (200.90 mM);Water: Insoluble;Ethanol: 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。 |
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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 | 3.5876 mL | 17.9379 mL | 35.8757 mL |
| 5 mM | 0.7175 mL | 3.5876 mL | 7.1751 mL |
| 10 mM | 0.3588 mL | 1.7938 mL | 3.5876 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。
The Rice BZ1 Locus Is Required for Glycosylation of Arabinogalactan Proteins and Galactolipid and Plays a Role in both Mechanical Strength and Leaf Color
Rice (N Y) 2020 Jun 17;13(1):41.PMID:32556633DOI:10.1186/s12284-020-00400-9.
Background: The cell wall and chloroplast are two fundamental structures determining plant mechanical strength and grain yield. Therefore, understanding mechanisms that improve plants' ability to develop a robust cell wall and well-developed chloroplast is of utmost importance for agricultural activities. Results: In this study, we report the functional characterization of a novel rice mutant, brittle stem and zebra leaf (BZ1), which displays altered cell wall composition and collapsed chloroplast membrane. Molecular and biochemical analysis revealed that BZ1 encodes a functional UDP-galactose/glucose epimerase (UGE) and is ubiquitously expressed with higher expression in stem and leaf tissues. Multiple techniques analyses, including immunoblots, immuno-gold, and cryogenic scanning electron microscopy, demonstrated a significantly impaired glycosylation of arabinogalactan proteins (AGPs) and disordered cellulose microfibril deposition in BZ1. Lipid profiling assay showed that the amount of monogalactosyldiacylglycerols (MGDG), a major chloroplast membrane glycolipid, was significantly decreased in BZ1. Taken together, these results strongly demonstrate that BZ1 participates in UDP-galactose supply for the sugar chains biosynthesis of AGPs and MGDG, which thereby, respectively, results in altered cell wall and abnormal chloroplast development. Due to inferior mechanical strength and reduced photosynthesis, BZ1 plants displayed detrimental agronomic traits, whereas BZ1 overexpressing lines showed enhanced plant growth. Transcriptome analysis of stems and leaves further showed that numerous key genes involved in AGPs biosynthesis and photosynthesis metabolism were substantially suppressed in BZ1. Conclusions: Our finding identifies BZ1 as a dual-targeting UGE protein for glycosylation of AGPs and MGDG and suggests a strategy for breeding robust elite crops.
Visualizing BZ1 missense suppression in Zea mays: an assay for monocot tRNA expression and utilization
Plant Mol Biol 2006 Jul;61(4-5):795-8.PMID:16897493DOI:10.1007/s11103-006-0050-7.
Bombardment of a highly expressed dicot tRNA(ala)(GAC) gene into Zea mays bz-E2 or bz-E5 coleoptiles causes suppression of an Ala(458 )-->Val missense mutation, visualized by the development of anthocyanin pigment. Missense suppression is blocked by mutation of tRNA(ala)(GAC) at a site that prevents aminoacylation by the dicot alanyl-tRNA synthetase, indicating that features identified for expression and utilization of dicot tRNAs also function in monocots. This assay of the expression and utilization of tRNA(ala)(GAC) also can be used to study a variety of tRNAs and their genes, most of which can be relatively easily altered to be charged by alanyl tRNA synthetase.
C1- and R-dependent expression of the maize BZ1 gene requires sequences with homology to mammalian myb and myc binding sites
Plant Cell 1991 Mar;3(3):317-25.PMID:1840914DOI:10.1105/tpc.3.3.317.
Tissue-specific expression of the maize anthocyanin Bronze-1 (BZ1) gene is controlled by the products of several regulatory genes. These include C1 or Pl and R or B that share homology to the myb proto-oncogenes and myc-like genes, respectively. BZ1 expression in embryo tissues is dependent on C1 and an R-sc allele of R. Transient expression from mutated and deleted versions of the BZ1 promoter fused to a luciferase reporter gene was measured in C1, Rscm2 embryos after gene transfer by microprojectiles. This analysis revealed that the sequences between -76 base pairs (bp) and -45 bp and a 9-bp AT-rich block between -88 bp and -80 bp were critical for BZ1 expression. The -76 bp to -45 bp region includes two short sequences that are homologous to the consensus binding sites of the myb- and myc-like proteins. Site-specific mutations of these "myb" and "myc" sequences reduced BZ1 expression to 10% and 1% of normal, respectively. Additionally, a trimer of a 38-bp oligonucleotide containing these myb and myc sites increased the expression of a cauliflower mosaic virus 35S minimal promoter by 26-fold. This enhancement was dependent on both C1 and R. Because the sites critical for BZ1 expression are homologous to the myb and myc consensus binding sequences and the C1 and R proteins share homology with the myb and myc products, respectively, we propose that C1 and R interact with the BZ1 promoter at these sites.
beta-Carboline-3-carboxylate-t-butyl ester: a selective BZ1 benzodiazepine receptor antagonist
Life Sci 1984 Nov 26;35(22):2227-36.PMID:6094935DOI:10.1016/0024-3205(84)90464-8.
The effectiveness of beta-carboline-3-carboxylate-t-butyl ester (beta CCtB) in antagonizing the anticonvulsant, ataxic and antipunishment effects of diazepam were evaluated. In mice, beta CCtB at doses of 3 and 10 mg/kg produced a dose-related antagonism of the anticonvulsant effects of diazepam against pentylenetetrazole (80 mg/kg). A dose of 30 mg/kg of beta CCtB did not produce a further shift in the diazepam dose-effect curve, apparently because beta CCtB failed to block the muscle-relaxant effects of diazepam. Further, beta CCtB (30 mg/kg) failed to antagonize the ataxic effects of diazepam in an inverted screen test. Rats responded under a multiple schedule where in one component every twentieth response (FR20) resulted in water presentation (unpunished component) and in another component every twentieth response (FR20) resulted in both shock and water presentation (punished component). Diazepam p.o. (0.1 to 10 mg/kg) first increased and then decreased rates in the punished component but only decreased rates in the unpunished component. beta CCtB had no effect on response rates when administered alone, but antagonized the rate-increasing effects of diazepam in the punished component. beta CCtB did not alter the rate-decreasing effects of diazepam in either component. Thus, beta CCtB selectively antagonized the effects of diazepam on punished behavior as well as the anticonvulsant effects of diazepam, but beta CCtB failed to antagonize the rate-decreasing and ataxic effects of diazepam. These results are consistent with the interpretation that beta CCtB is a selective BZ1 benzodiazepine receptor antagonist.
The GABA(A) receptor complex in the chicken brain: immunocytochemical distribution of alpha 1- and gamma 2-subunits and autoradiographic distribution of BZ1 and BZ2 binding sites
J Chem Neuroanat 2003 Jan;25(1):1-18.PMID:12573455DOI:10.1016/s0891-0618(02)00071-6.
Two antibodies, raised against the rat GABA(A) receptor alpha1- and gamma2-subunits, were used for an immunocytochemical study of the distribution of these proteins in the chicken brain. The immunoreactive bands obtained by Western blotting and the similar labelling distribution found in the rat and chicken brain support the suitability of these antibodies for the labelling of GABA(A) receptors in birds. We found abundant alpha1 and gamma2 immunoreactivity throughout the chicken brain, mainly in the paleostriata and lobus paraolfactorius, dorsal thalamus and some nuclei of the brainstem. The alpha1-subunit was more abundant in the telencephalon, thalamus and cerebellum, while the presence of the gamma2-subunit was stronger in the optic tectum and brainstem. We also report the autoradiographic distribution of the BZ1 and BZ2 benzodiazepine receptor subtypes in the chicken brain using [3H]flunitrazepam. Benzodiazepine binding was unevenly distributed throughout the chicken brain, and the anatomical distribution of the BZ1 and BZ2 subtypes was similar to that described in mammals. The highest binding values were found in the olfactory bulb, paleostriatum primitivum, optic tectum, nucleus mesencephalicus lateralis pars dorsalis and nucleus isthmi pars parvocellularis, the BZ2 subtype being predominant in the paleostriatum primitivum and optic tectum. A general agreement in the distribution of BZ1 and alpha1 immunoreactivity was observed in structures such as the olfactory bulb, paleostriata, lobus parolfactorius and dorsal thalamus, although some discrepancies were observed in areas such as the optic tectum or nucleus isthmi pars parvocellularis, with high BZ1 binding and low or no alpha1 immunolabelling.