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AZ2 Sale

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。

AZ2 Chemical Structure

Cas No.:2231760-33-9

规格 价格 库存 购买数量
10mM (in 1mL DMSO)
¥2,970.00
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5 mg
¥2,700.00
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10 mg
¥4,320.00
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25 mg
¥8,550.00
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50 mg
¥13,050.00
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100 mg
¥20,250.00
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产品描述

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.

Chemical Properties

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
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溶解性数据

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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
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Research Update

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.