ANP32B
- Known as:
- ANP32B
- Catalog number:
- 001679A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ANP32B
Related genes to: ANP32B
- Gene:
- ANP32B NIH gene
- Name:
- acidic nuclear phosphoprotein 32 family member B
- Previous symbol:
- -
- Synonyms:
- SSP29, PHAPI2, APRIL
- Chromosome:
- 9q22.33
- Locus Type:
- gene with protein product
- Date approved:
- 2002-02-13
- Date modifiied:
- 2016-10-05
Related products to: ANP32B
Related articles to: ANP32B
- Understanding the molecular mechanisms driving H5N1 clade 2.3.4.4b is critical for pandemic preparedness. - Source: PubMed
Publication date: 2026/07/14
Lee SangyiCho SeunghyeKim HyunbeenShin WoojinLee SoyoungDemirev Atanas VKim Jin Il - Seasonal influenza in humans is predominantly caused by influenza A virus (IAV) and influenza B virus (IBV), but they differ markedly in host range, evolutionary dynamics, and pandemic potential. Such phenotypic divergence reflects the distinct molecular strategies employed by the two viruses at key stages of their life cycles. Hemagglutinin (HA) of IAV possesses prominent structural plasticity, which endows it with the capacity to recognize both avian-type α2,3-linked and human-type α2,6-linked sialic acid receptors, and the function of IAV polymerase is highly dependent on host acidic nuclear phosphoprotein 32 (ANP32) family proteins. Moreover, IAV utilizes multiple pleiotropic virulence factors, such as the nonstructural protein 1 (NS1), to modulate host immune responses and inflammatory processes, thereby contributing to viral fitness, host adaptation, and pandemic potential. In contrast, the HA of IBV preferentially binds to human-type (α2,6-linked) sialic acid receptors and exhibits a more restricted receptor-binding profile.While IBV polymerase is well adapted to human ANP32A and ANP32B, yet shows poor compatibility with avian ANP32 proteins. Additionally, the immunomodulatory machinery is relatively streamlined, engaging host cell death pathways in a more limited manner that may contribute to generally less extensive inflammatory responses in many experimental and clinical settings. As a result, IBV transmission is largely confined to humans, with a narrow host range and a predominantly seasonal epidemic pattern. In this review, we systematically compare IAV and IBV with respect to four core pathogenic processes, namely viral entry, genome replication efficiency and host factor dependence, immune evasion, and the regulation of host cell death pathways, to explain how these mechanisms collectively shape differences in host range, evolutionary dynamics, and pandemic potential. We particularly emphasize the capacity of IAV to achieve efficient replication in a wide range of host species, a trait that facilitates its multi-host circulation and viral gene reassortment. These insights establish a theoretical framework for enhancing influenza surveillance and guiding the development of next-generation influenza vaccines and antiviral therapeutics. - Source: PubMed
Publication date: 2026/07/09
Zhang XiaoyangTang QinZhang YongleGuo JianchaoYao XuejieLuo ZhongGuo XinyuZhao YueZhu HenghuiLiu ChangHuang CanHou ZiyingYang ChendiChen RuiqiMa Jiaqi - Acute myeloid leukemia (AML) is a severe and life-threatening malignant disease of the hematopoietic system. Our previous research found that ANP32B is regulated by super enhancers in pediatric AML and regulates the progression of AML by modulating histone H3K27ac. Using virtual screening technology, we discovered that Raloxifene may be a small-molecule inhibitor targeting ANP32B. - Source: PubMed
Publication date: 2026/06/29
Wan XiaomeiYu ZhongHuang ChengchengRen Ying - Eradicating leukemic stem cells (LSCs), a major driver of primary resistance and relapse in chronic myeloid leukemia (CML) following tyrosine kinase inhibitor (TKI) treatment, is critical for achieving a cure. Previously, we identified that ANP32B promotes CML LSCs' survival and leukemogenesis by directly binding and inhibiting p53 activity, suggesting a therapeutic opportunity. Here, we show that 1-amino-8-naphthol-2,4-disulfonic acid (ANDS) binds unacetylated p53 and restores p53 activity by disrupting ANP32B-p53 interaction. Consequently, ANDS inhibits CML cell proliferation, impairs LSC function and prolongs survival in the CML mouse model while sparing normal progenitor cells. Based on notion that ANDS, as a previously-identified CaMKP inhibitor, potentially activates p-CaMKIIγ to accelerate CML progression, we find that ANDS combination with KN93, a p-CaMKIIγ inhibitor, synergistically suppresses both TKI-sensitive and -resistant CML. Thus, we highlight that ANDS alone or in combination with CaMKP inhibitor could become a therapeutic strategy for eradicating LSCs and overcoming TKI-resistance in CML. - Source: PubMed
Publication date: 2026/06/10
Wei Yu-ShengJin Fei-YuZeng Hong-HuiLiu Hao-RanChen Ying-YiWu Ying-LiZhou Ai-WuZhang JianYu YunChen Guo-Qiang - The species-specific acidic nuclear phosphoprotein 32 kDa members (ANP32A/B) play a key role in restricting the function of avian influenza virus polymerase in mammalian host. Avian influenza viruses, upon replicating in humans, may acquire critical amino acid substitutions in the polymerase basic 2 (PB2) protein (e.g. E627 K and D701N) that enhance the viral polymerase's functional compatibility with human ANP32A and ANP32B proteins, thereby augmenting viral replication efficiency and increasing pathogenic potential in humans. However, certain H5N1 avian influenza viruses have demonstrated the capacity to establish productive human infections in the absence of the canonical PB2-627 K or PB2-701N adaptive mutations; the underlying molecular mechanism remains incompletely characterized. In this study, we found that the two H5N1 viruses, namely A/chicken/LN/SD035/2018 (LN35) and A/duck/JL/S1261/2019 (JL261), were genetically similar, but their pathogenicity for mice was different. By evaluating a series of single-gene reassortant viruses and mutants in mice, we confirmed that the PB2-384L/443R/460M characteristics are crucial for LN35 to maintain high lethality in mice. We further revealed that the polymerase of H5N1 avian virus bearing PB2-384L/443R/460M signature could efficiently utilize human ANP32A/B. Moreover, we found that this PB2-384L/443R/460M signature positively regulates H5N1 vRNP-human ANP32A/B interaction and vRNP assembly. Our findings indicate that key amino acid substitutions in the PB2 gene of the H5N1 virus may emerge in avian host and then augment its capacity to interact with human ANP32A/B protein, underscoring the substantial zoonotic and public health risks associated with continued circulation and evolution of H5N1 in avian populations. - Source: PubMed
Publication date: 2026/06/21
Lin WeipengDeng GuohuaXing XinShi JianzhongKong HuihuiLiu LilingZeng XianyingJiang LiLi ChengjunGuan YuntaoCui PengfeiChen Hualan