Polyclonal Rabbit ATXN2L Antibody
- Known as:
- Polyclonal Rabbit ATXN2L Antibody
- Catalog number:
- KA0352
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit ATXN2L Antibody
Related genes to: Polyclonal Rabbit ATXN2L Antibody
- Gene:
- ATXN2L NIH gene
- Name:
- ataxin 2 like
- Previous symbol:
- -
- Synonyms:
- A2lp, A2D
- Chromosome:
- 16p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-08-18
- Date modifiied:
- 2016-10-05
Related products to: Polyclonal Rabbit ATXN2L Antibody
Related articles to: Polyclonal Rabbit ATXN2L Antibody
- Translation initiation in eukaryotic cells is usually driven by recognition of a 5' cap and a 3' poly(A) tail, which cooperate through interactions with eukaryotic initiation factors (eIFs) and poly(A)-binding protein (PABP) to promote mRNA circularization and efficient ribosome recruitment. However, many viral RNAs lack one or both of these canonical features and must use alternative strategies to access the host translational machinery. Diverse mechanisms are used to bypass cap dependence, including internal ribosome entry sites that recruit ribosomal subunits with variable requirements for canonical initiation factors as well as viral protein genome-linked strategies that functionally substitute for the cap by engaging components of the eIF4F complex. For viral mRNAs lacking poly(A) tails, translation can be supported by long-range RNA-RNA interactions that mediate 5'-3' communication and viral or host proteins that replace PABP to facilitate closed-loop formation. Emerging examples, including host protein ATXN2L during reovirus infection, illustrate how viruses use or mimic cellular factors to promote selective translation. Collectively, these strategies reveal fundamental principles of mRNA circularization and translational control, highlighting the dynamic interplay between viral and host machinery in regulating protein synthesis. - Source: PubMed
Publication date: 2026/05/08
Somoulay XayathedTaylor Gwen MDermody Terence S - The c-Jun N-terminal kinase (JNK) pathway is an evolutionarily conserved signaling cascade that regulates development, stress responses, and pathogenesis. While aberrant JNK activation is linked to cancer and neurodegeneration, its regulatory mechanisms are not fully understood. Here, we identify the RNA-binding protein Ataxin-2 (Atx2) as a novel, essential regulator of JNK-mediated cell death and migration in Drosophila. Atx2 deficiency suppressed JNK-dependent apoptosis, tumor growth and invasion, and thorax closure in normal development, while its overexpression activated JNK signaling, promoting cell death, migration, and tissue remodeling. Mechanistically, Atx2 binds the 3' UTR of hipk mRNA, stabilizing it to enhance the expression of Hipk, a core upstream JNK kinase. Strikingly, this mechanism is conserved: human ATXN2L potently activated Hipk-JNK signaling and cell death in Drosophila and HeLa cells. Our findings reveal a conserved post-transcriptional mechanism for JNK pathway regulation and nominate Atx2 family proteins as potential therapeutic targets in JNK-associated pathologies. - Source: PubMed
Publication date: 2026/05/02
Li XinyaoZhu XiaojieLi WenzheDeng HansongXue Lei - Anaplastic large cell lymphoma (ALCL) is a rare form of mature T cell lymphoma in children, particularly the anaplastic large cell kinase (ALK) negative subtype. Despite frontline treatment advances, there is no standard approach to treat relapsed disease and prognosis remains poor. Recently, JAK/STAT activating mutations have been implicated in the pathogenesis of ALK-negative ALCL in adults, but the oncogenic drivers of this disease in children are not well characterized. Herein, we describe a case of a 13 year-old boy with early systemic relapse of ALK-negative ALCL harboring a rare ATXN2L::JAK2 fusion, who achieved complete remission with ruxolitinib monotherapy. Consolidative allogeneic hematopoietic stem cell transplant HSCT then lead to long-term remission. This case underscores the critical role of comprehensive genomic profiling for rare histologies and supports the potential utility of JAK/STAT pathway inhibitors in select patients with ALK-negative ALCL. - Source: PubMed
Publication date: 2026/02/14
Cohen TalZhou TingEdema UkuemiPandit-Taskar NeetaForlenza ChristopherPrice AnitaRamaswamy KavithaTrippett TanyaSulis Maria LuisaBoelens Jaap-JanLim Megan SShukla Neerav - Polyglutamine expansion in Ataxin-2 (ATXN2) is responsible for rare, dominantly inherited Spinocerebellar Ataxia type 2 (SCA2). Together with its paralog Ataxin-2-like (ATXN2L), both proteins have received much interest, since the deletion of their yeast and fly orthologs alleviates TDP-43-triggered neurotoxicity in Amyotrophic Lateral Sclerosis models. Their typical structure across evolution combines LSm with LSm-Associated Domains and a PAM2 motif. To understand the physiological regulation and functions of Ataxin-2 homologs, the phylogenesis of sequences was analyzed. Human ATXN2 harbors multiple alternative start codons, e.g., from an intrinsically disordered sequence (IDR) present since armadillo, or from the polyQ sequence that arose since amphibians, or from the LSm domain since primitive eukaryotes. Multiple smaller isoforms also exist across the C-terminus. Therapeutic knockdown of polyQ expansions in human ATXN2 should selectively target exon 1B. PolyQ repeats developed repeatedly, usually framed and often interrupted by (poly)Pro, originally near PAM2. The LSmAD sequence appeared in algae as the characteristic Ataxin-2 feature with strong conservation. Frequently, Ataxin-2 has added domains, likely due to transcriptional readthrough of neighbor genes during cell stress. These chimerisms show enrichment of rRNA processing; nutrient store mobilization; membrane strengthening via lipid, protein, and glycosylated components; and cell protrusions. Thus, any mutation of Ataxin-2 has complex effects, also affecting membrane resilience. - Source: PubMed
Publication date: 2026/02/03
Auburger Georg W JKey JanaGispert SuzanaLastres-Becker IsabelAlmaguer-Mederos Luis-EnriqueBassa CaroleAuburger AntoniusAuburger GeorgArsovic AleksandarDeller ThomasSen Nesli-Ece - The Ataxin-2 protein (ATXN2) plays an essential role in RNA metabolism and many cellular processes. Dysregulation or mutation of the gene () can lead to neurodegenerative diseases such as spinocerebellar ataxia type 2 (SCA2) and amyotrophic lateral sclerosis (ALS). Despite numerous efforts in this field in other animal models, little is known about Atxn2 in zebrafish. In this study, we aim to investigate the potential suitability of zebrafish as a model for Atxn2-related diseases by performing basic analyses on Atxn2. We performed a bioinformatic protein analysis of Atxn2 from zebrafish and its paralog Atxn2l in relation to human and other vertebrate homologues. Based on a structural analysis of the and genes, the expression of the predicted transcripts was detected by RT-PCR and the spatiotemporal expression pattern was determined by whole-mount in situ hybridization. We found similarities between the protein sequences of Atxn2 and Atxn2l in zebrafish and their functional domains with those of orthologs in humans and other vertebrates. The predicted transcripts of and were experimentally verified and their spatiotemporal expression patterns were determined during zebrafish development. Splicing variants were detected for both genes, suggesting a different role for the isoforms in different tissues. These findings provide new insights into the and genes, suggesting the zebrafish as a suitable animal model for functional studies and research on disease modeling of SCA2 and ALS. - Source: PubMed
Publication date: 2025/12/03
Vauti FranzEilers LukasKroll AnnekeKöster Reinhard W