KPNA6
- Known as:
- KPNA6
- Catalog number:
- Y213970
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- KPNA6
Related genes to: KPNA6
- Gene:
- KPNA6 NIH gene
- Name:
- karyopherin subunit alpha 6
- Previous symbol:
- -
- Synonyms:
- IPOA7, KPNA7, MGC17918, FLJ11249
- Chromosome:
- 1p35.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-12-14
- Date modifiied:
- 2016-10-05
Related products to: KPNA6
anti-KPNA6 (Internal)Anti-KPNA6, Goat Polyclonal to KPNA6, Isotype , Host GoatAntibodies: KPNA6 HOST: Goat Clonality: pAbBovine Importin subunit alpha-7 (KPNA6) ELISA KitBovine Importin subunit alpha-7 (KPNA6) ELISA KitBovine Importin subunit alpha-7 (KPNA6) ELISA KitBovine Importin subunit alpha-7(KPNA6) ELISA kitBovine Importin subunit alpha-7(KPNA6) ELISA kit SpeciesBovineBovine karyopherin alpha 6 (importin alpha 7) (KPNA6) ELISA kit, Species Bovine, Sample Type serum, plasmaELISA Kit FOR Importin subunit alpha-7; organism: Mouse; gene name: Kpna6GOAT ANTI HUMAN KPNA6 Polyclonal Antibody Host: Goat Polyclonal IgGGOAT ANTI HUMAN KPNA6, Product Type Polyclonal Antibody, Specificity KPNA6, Target Species Human, Host Goat, Format Purified, Isotypes Polyclonal IgG, Applications E, WB, CloneGOAT ANTI HUMAN KPNA6, Product Type Polyclonal Antibody, Specificity KPNA6, Target Species Human, Host Goat, Format Purified, Isotypes Polyclonal IgG, Applications E, WB, CloneGOAT ANTI HUMAN KPNA6-POLYCLONAL ANTIBODYGoat Anti-Human KPNA6, (internal) Antibodies Related articles to: KPNA6
- Molting is a critical physiological process for the growth and development of . Any disruption in this process can significantly affect both survival rates and crab quality. The regulatory mechanisms of molting vary across different stages of the molting cycle and remain poorly understood. In this study, ATAC-seq and RNA-seq were combined to identify the integrated differentially expressed genes (IDEGs) in muscle across adjacent stages of the molting cycle. A total of 17, 491, 84, and 491 IDEGs were identified in the comparisons of inter-molt_vs_pre-molt, pre-molt_vs_molt, molt_vs_post-molt, and post-molt_vs_inter-molt stages, respectively. GO enrichment analysis of these IDEGs revealed several key signaling pathways involved in each adjacent molting stage. The GPCR signaling, steroid hormone-mediated signaling, and smoothened signaling pathways were all active across three molting transitions (pre-molt_vs_molt, molt_vs_post-molt, and post-molt_vs_inter-molt). Among them, the GPCR pathway played a dominant role throughout the process. Further structural analysis and RT-qPCR validation identified eight GPCRs involved in molting regulation: and were specific to the post-molt_vs_inter-molt stage; , , and were unique to the pre-molt_vs_molt stage; and functioned in both post-molt_vs_inter-molt and pre-molt_vs_molt stages; and was active in both post-molt_vs_inter-molt and molt_vs_post-molt stages. These findings improve the understanding of molting regulation and provide potential targets for further genetic improvement in . - Source: PubMed
Publication date: 2026/01/08
He ZhenLi JingjingZhang JingjingZhang RuiqiTan RongkangSun JinshengWang BinHao Tong - Highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV) is a mutant strain of the classic porcine reproductive and respiratory syndrome virus (PRRSV) characterized by high morbidity and mortality rates. Epidemiological analysis revealed a natural mutation and stable inheritance of amino acid 46 (41-PGKKNKK-47 mutated to 41-PGKKNRK-47) in the nuclear localization signal or sequence (NLS) region of the N protein of HP-PRRSV. In this study, we showed that the nucleoplasmic shuttling of the HP-PRRSV N protein was associated with a higher efficiency of viral replication than that of the classical PRRSV. The nuclear transporter receptors KPNB1, KPNA1, KPNA2, KPNA6, and KPNA7 were involved in the nuclear import of the N protein. Additionally, the mRNA expression levels of KPNB1 and KPNA1 differed between the two strains after infecting the Marc-145 cells with these strains. The viral replication efficiency also decreased when expression levels of KPNA1 and/or KPNB1 were lowered. Finally, protein binding simulation and kinetic assay showed that the mutation of key amino acid 46 in the NLS region altered the binding mode and kinetics of the N proteins to KPNA1 and KPNB1. This study elucidates, for the first time, the reasons for the enhanced nucleoplasmic shuttling and replication efficiency of HP-PRRSV from the perspective of protein entry into the nucleus. It also provides a foundational reference for the prevention and control of PRRSV. - Source: PubMed
Publication date: 2025/07/04
Zhu XianchangXia YangLei QianGan YuJiang ShenghaiHuang LianWen QihuFu WeiZhang BoZhang YiXie ShanshanLi Jida - The conversion of white adipose tissue (WAT) to brown adipose tissue (BAT) is a promising strategy for obesity treatment. It is previously identified βFaar as a conserved long noncoding RNA (lncRNA) regulator of islet β-cell function in individuals with obesity, but its effect on WAT browning is not well understood. In this study, it is discovered that βFaar expression in adipose tissue markedly decreases with the progression of obesity in both mice and humans. βFaar in adipose tissue reduces lipid droplet (LD) size in WAT and promotes a browning phenotype in inguinal WAT (iWAT), leading to the amelioration of high-fat diet (HFD)-induced obesity. These effects can be attributed to crosstalk between βFaar and proteins within the master regulatory pathways of LD formation and WAT browning, including RAS oncogene family 18 (RAB18) and interferon regulatory factor 4 (IRF4). Specifically, βFaar inhibits LD swelling by binding to RAB18 and promoting IRF4 nuclear translocation, increases uncoupling protein 1 (UCP1) transcription, and further induces iWAT browning by binding to karyopherin subunit alpha 6 (KPNA6). Together, these results demonstrate the critical roles of βFaar in regulating iWAT browning and preserving metabolic health; thus, βFaar may be a potential therapeutic target for management of obesity and related disorders. - Source: PubMed
Publication date: 2025/06/23
Yang YueHuang BinSha BaixueGao DanniQin YimengLi ZiyiChen XiJin YinuoPan YiZhang YanfengShen YumengLiu YuJin LiangZhang Fangfang - The abundance of a protein is defined by its continuous synthesis and degradation, a process known as protein turnover. Here, we systematically profiled the turnover of proteins in influenza A virus (IAV)-infected cells using a pulse-chase stable isotope labeling by amino acids in cell culture (SILAC)-based approach combined with downstream statistical modeling. We identified 1,798 virus-affected proteins with turnover changes (tVAPs) out of 7,739 detected proteins (data available at pulsechase.innatelab.org). In particular, the affected proteins were involved in RNA transcription, splicing and nuclear transport, protein translation and stability, and energy metabolism. Many tVAPs appeared to be known IAV-interacting proteins that regulate virus propagation, such as KPNA6, PPP6C, and POLR2A. Notably, our analysis identified additional IAV host and restriction factors, such as the splicing factor GPKOW, that exhibit significant turnover rate changes while their total abundance is minimally affected. Overall, we show that protein turnover is a critical factor both for virus replication and antiviral defense. - Source: PubMed
Publication date: 2024/10/04
Huang YiqiUrban ChristianHubel PhilippStukalov AlexeyPichlmair Andreas - Cryptorchidism (CO) is a risk factor for the development of testicular germ-cell tumors (TGCT). This is supported by reports showing the persistence of gonocytes in CO patients. These cells are proposed to be related to the development of germ-cell neoplasia in situ (GCNIS), which is considered the precursor stage/lesion of TGCT. Therefore, it is proposed that some patients with CO could express some molecular markers related to TGCT. In this study, we analyzed testicular tissue samples from CO, TGCT, and controls. We determined the expression of POU5F1, PLAP, and KIT by immunohistochemistry and that of the hsa-miR-371-373 cluster, hsa-miR-367, and , , and genes by RT-qPCR. We then carried out a bioinformatic analysis to identify other possible candidate genes as tumor biomarkers. We found that 16.7% (2/12) of the CO patients presented increased expression of POU5F1, KIT, PLAP, hsa-miR-371-373, and hsa-miR-367 and decreased expression of and . Finally, the genes , , and were identified as other possible candidate tumor biomarkers. This is the first report describing the expression of the hsa-miR-371-373 cluster, hsa-miR-367, , and in the testicular tissues of two CO patients with cells immune-positive to POU5F1, PLAP, and KIT, which is similar to what is observed in TGCT. - Source: PubMed
Publication date: 2023/09/21
García-Andrade FabiolaVigueras-Villaseñor Rosa MaríaChávez-Saldaña Margarita DoloresRojas-Castañeda Julio CésarBahena-Ocampo Ivan UrielAréchaga-Ocampo ElenaFlores-Fortis MauricioDíaz-Chávez JoséHerrera Luis AlonsoLandero-Huerta Daniel Adrian