AZ2
目录号 : GC62335
AZ2 是一种高度选择性的 PI3Kγ 抑制剂（PI3Kγ 的 pIC50 为 9.3）。AZ2 可用于炎症和免疫疾病的研究。
Cas No.:2231760-33-9
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >99.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
AZ2 is a highly selective PI3Kγ inhibitor (The pIC50 value for PI3Kγ is 9.3). AZ2 can be used for the research of inflammatory and immune diseases[1].
AZ2 (0.1~100 nM; 1 hour; SKOV-3 cells) excellent selectivity for PI3Kγ is further confirmed with a constitutively activated PI3K/Akt pathway[1].
[1]. Gangadhara G, et al. A class of highly selective inhibitors bind to an active state of PI3Kγ. Nat Chem Biol. 2019;15(4):348-357.
| Cas No. | 2231760-33-9 | SDF | |
| 分子式 | C20H23N3O2S | 分子量 | 369.48 |
| 溶解度 | DMSO : 50 mg/mL (135.33 mM; Need ultrasonic) | 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 | 2.7065 mL | 13.5325 mL | 27.0651 mL |
| 5 mM | 0.5413 mL | 2.7065 mL | 5.413 mL |
| 10 mM | 0.2707 mL | 1.3533 mL | 2.7065 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。
Subcellular localization and phosphorylation of antizyme 2
J Cell Biochem 2009 Nov 1;108(4):1012-21.PMID:19725046DOI:10.1002/jcb.22334.
Antizymes (AZs) are polyamine-induced proteins that negatively regulate cellular polyamine synthesis and uptake. Three antizyme isoforms are conserved among mammals. AZ1 and AZ2 have a broad tissue distribution, while AZ3 is testis specific. Both AZ1 and AZ2 inhibit ornithine decarboxylase (ODC) activity by binding to ODC monomer and target it to the 26S proteasome at least in vivo. Both also inhibit extra-cellular polyamine uptake. Despite their being indistinguishable by these criteria, we show here using enhanced green fluorescent protein (EGFP)-AZ2 fusion protein that in mammalian cells, the subcellular location of AZ2 is mainly in the nucleus, and is different from that of AZ1. The C-terminal part of AZ2 is necessary for the nuclear distribution. Within a few hours, a shift in the distribution of EGFP-AZ2 fusion protein from cytoplasm to the nucleus or from nucleus to cytoplasm is observable in NIH3T3 cells. In addition, we found that in cells a majority of AZ2, but not AZ1, is phosphorylated at Ser-186, likely by protein kinase CK2. There may be a specific function of AZ2 in the nucleus.
Novel ubiquitin-independent nucleolar c-Myc degradation pathway mediated by antizyme 2
Sci Rep 2018 Feb 14;8(1):3005.PMID:29445227DOI:10.1038/s41598-018-21189-0.
The proto-oncogene c-Myc encodes a short-lived protein c-Myc that regulates various cellular processes including cell growth, differentiation and apoptosis. Degradation of c-Myc is catalyzed by the proteasome and requires phosphorylation of Thr-58 for ubiquitination by E3 ubiquitin ligase, Fbxw7/ FBW7. Here we show that a polyamine regulatory protein, antizyme 2 (AZ2), interacts with c-Myc in the nucleus and nucleolus, to accelerate proteasome-mediated c-Myc degradation without ubiquitination or Thr-58 phosphorylation. Polyamines, the inducer of AZ2, also destabilize c-Myc in an AZ2-dependent manner. Knockdown of AZ2 by small interfering RNA (siRNA) increases nucleolar c-Myc and also cellular pre-rRNA whose synthesis is promoted by c-Myc. AZ2-dependent c-Myc degradation likely operates under specific conditions such as glucose deprivation or hypoxia. These findings reveal the targeting mechanism for nucleolar ubiquitin-independent c-Myc degradation.
On the system of Diophantine equations x2 - 6y2 = -5 and x = AZ2 - b
ScientificWorldJournal 2014;2014:632617.PMID:25045739DOI:10.1155/2014/632617.
Mignotte and Pethö used the Siegel-Baker method to find all the integral solutions (x, y, z) of the system of Diophantine equations x (2) - 6y (2) = -5 and x = 2z (2) - 1. In this paper, we extend this result and put forward a generalized method which can completely solve the family of systems of Diophantine equations x (2) - 6y (2) = -5 and x = az (2) - b for each pair of integral parameters a, b. The proof utilizes algebraic number theory and p-adic analysis which successfully avoid discussing the class number and factoring the ideals.
Isolation of the novel cDNA of a gene of which expression is induced by a demethylating stimulus
Gene 1999 Nov 29;240(2):289-95.PMID:10580148DOI:10.1016/s0378-1119(99)00450-3.
We have isolated a novel cDNA clone, named AZ2, from a cDNA library of mRNA prepared from C3H10T1/2 cells that had been transiently exposed to 5-azacytidine, a potent inhibitor of DNA methyltransferase. The elucidated nucleotide sequence revealed that the 5' region of the cDNA was rich in the CpG sequence. The AZ2 cDNA contained a 1215-nucleotide open reading frame, and the expected amino acid sequence had a molecular mass of 46090. The amount of the transcript increased on 5-azacytidine treatment of C3H10T1/2 cells, and the transcript was significantly expressed in mouse testis, brain, lung, kidney, heart and ovary. Specific antibodies raised against a fusion protein including glutathione S-transferase revealed a band of an approximately 48kDa translation product for testis, brain, lung, and cultured cells that ectopically expressed the AZ2 protein. The AZ2 protein was mainly localized in the cytoplasm. The amino-terminal part of the AZ2 protein was homologous to the previously reported TANK (Cheng and Baltimore, 1996. Genes Dev. 10, 963-973) and I-TRAF (Rothe, 1996. Proc. Natl. Acad. Sci. USA 93, 8241-8246), which participate in the signal transduction cascade from the tumor necrosis factor-receptor to the transcription factor, NFkappaB. Overexpression of AZ2 inhibited TNF alpha mediated NFkappaB activation. AZ2 could be a component of a regulator of the NFkappaB activation cascade.
Cloning and expression of AZ2, a putative zinc finger transcription factor from Drosophila melanogaster
Dev Genes Evol 1998 May;208(3):172-4.PMID:9601993DOI:10.1007/s004270050171.
A Drosophila gene (AZ2), mapping to a cluster of embryonic lethals at 43BC on the polytene chromosomes, has been sequenced and found to encode a predicted protein with six consecutive C2H2 zinc finger domains. The carboxy-terminus of AZ2 is related to a number of Drosophila and mammalian transcription factors. The 5' end of the gene is unrelated to genes in the databases. The gene is expressed in the adult female, in both the carcass and ovary, but is most abundant in the ovary. It is expressed in the nurse cells and transported to the oocyte.