TUBA4A Antibody
- Known as:
- TUBA4A Antibody
- Catalog number:
- abx000663
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- TUBA4A Antibody
Related genes to: TUBA4A Antibody
- Gene:
- TUBA4A NIH gene
- Name:
- tubulin alpha 4a
- Previous symbol:
- TUBA1
- Synonyms:
- FLJ30169, H2-ALPHA
- Chromosome:
- 2q35
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-10-05
Related products to: TUBA4A Antibody
Related articles to: TUBA4A Antibody
- Hereditary ataxias are a heterogeneous group of neurodegenerative disorders characterized by impaired balance and coordination, often due to cerebellar dysfunction. Despite advances in identifying genetic causes, animal models remain essential for dissecting underlying mechanisms and testing therapeutic strategies. Here we describe a mouse model of spastic ataxia and myopathy caused by a missense mutation in Tuba4a (n.A626C, p.Gln176Pro). In an ENU mutagenesis screen, a male C57BL/6 J mouse exhibiting muscle wasting and an intention tremor starting at approximately 4 weeks-of-age was identified. The male was bred by in vitro fertilization to BALB/cByJ oocyte donors. Genetic mapping determined dominant inheritance and localized the mutation to Chromosome 1. Genome sequencing revealed single nucleotide polymorphisms (SNPs) in serine threonine kinase 36 (Stk36Y1003N) and alpha-tubulin 4A (Tuba4aQ176P) in the mapping interval. These SNPs were CRISPR-engineered into C57BL/6 J mice, which confirmed the Tuba4aQ176P variant as the causative mutation. Mutant mice are normal at 3 weeks, except for decrement in muscle response following repetitive nerve stimulation. However, by 30 days these mice have overt ataxia, Purkinje neuron degeneration, and extensive skeletal muscle defects, which contribute to a decreased lifespan. Dominant TUBA4A mutations in humans are associated with spastic ataxia type 11 (SPAX11), congenital myopathy type 26 (CMYO26), and frontotemporal dementia/amyotrophic lateral sclerosis type 9 (FTDALS9). Our mice exhibit hallmark features of SPAX11 and CMYO26, but do not show motor neuron degeneration. This specificity makes this model a valuable tool for studying cell-type selective effects of TUBA4A mutations in neurodegeneration and myopathy. - Source: PubMed
Hines Timothy JFunke Jonathan RPratt Samia LRice Alaura DTwiss Jeffery LBurgess Robert W - Follicular fluid forms the essential microenvironment for oocyte growth and maturation, with its molecular features tightly correlated with oocyte developmental competence. Elucidating molecular differences in follicular fluid among follicles of different diameters is crucial for deciphering the mechanisms governing follicular development. - Source: PubMed
Publication date: 2026/07/30
Jiang LileYang ShujunWang YiwenXie JuankeGeng JiaxuanZhang HelongZhang YixuanWang QianChen YixuanWang XingyiZhang Cuilian - Prostate cancer is one of the most common malignant tumors of the male genitourinary system. The impaired activity of natural killer (NK) cells observed in prostate cancer may contribute to immune evasion. This study aimed to develop robust NK cell-related diagnostic signatures. - Source: PubMed
Publication date: 2026/06/03
Chen ZhengjunZhou FangTian JingzhiLv QianWang DongFan Shida - : Systemic lupus erythematosus is a complex autoimmune disease characterized by immune dysregulation and multisystem involvement. The primary cilium, a crucial cellular sensory organelle involved in immune signaling, has received limited attention in SLE. This study aims to characterize the expression patterns and potential regulatory features of primary cilium-related molecules in SLE and explore candidate compounds through integrated proteomic and phosphoproteomic analysis. : Proteomic and phosphoproteomic data were obtained from peripheral blood mononuclear cells of 130 SLE patients and 90 healthy controls. Gene ontology enrichment and hierarchical clustering analysis were used to characterize functional features and expression patterns of primary cilium-related molecules. PPI network analysis and phosphosite annotation were used to identify hub proteins and key phosphorylation sites (phosphosites). Stage-associated regulatory features were explored using Mfuzz clustering and kinase-substrate network analysis. Candidate compounds were predicted Connectivity Map (cMAP). : A total of 67 differentially expressed and 36 differentially phosphorylated primary cilium-related proteins were identified. The PPI network identified hub proteins (MAPRE1, VCP, TUBB, TUBB4B and RAB7A) and key phosphosites (TUBB S168/S172, TUBA4A S48 and SEPTIN2 S218). Kinase analysis highlighted that IKKβ, GSK3β and CDK5 were associated with stable-stage patterns, whereas MAP2K2, CDKL1 and CCRK were associated with active-stage patterns. Increased predicted IKKβ activity, elevated CYLD S422 phosphorylation and upregulated NF-κB1/2 expression in SLE suggested the potential involvement of a candidate IKKβ-CYLD/NF-κB regulatory module. Stage-associated cMAP analysis identified 20 candidate compounds with potential reversal signatures. : This study suggests a primary cilium-related regulatory network in SLE and identifies hub proteins, key phosphosites and kinases associated with stage-related molecular patterns. These findings provide new insights into primary cilium-related molecular alterations in SLE and propose preliminary candidate compounds that require further validation. - Source: PubMed
Publication date: 2026/07/27
Wei MengqiZhang QinxinXue HaoTang DongeDai YongZhang Wei - The C-terminal tails (CTTs) of αβ-tubulin heterodimer are intrinsically disordered regions (IDRs) which play critical roles in regulating the processivity and velocity of kinesin walking along microtubule. However, their involvement in the binding process of kinesin to microtubule remains poorly understood. To seek the binding process, a kinesin with high binding ability, KIF7 and its partner microtubule TUBA4A-TUBB8 complex were chosen. They were employed biphasic steered and long-term all-atom molecular dynamic simulation to study the CTTs' conformational changes induced by kinesin recruitment. We propose that the disordered CTTs extend outward to capture the surrounding kinesin. It then gradually transitions into α-helical conformation, stabilizing kinesin-microtubule interactions, akin to molecular glue. Further computationally biophysical analyses, including electrostatic analyses and binding free energies, showed that CTTs enhanced the binding affinity between kinesin and microtubule. Additionally, high-occupancy hydrogen bonds were such as arginine 308 in kinesin and glutamine 410 in β-tubulin when CTTs were present, which contributed to the protein-protein interactions. Our findings provide atomistic insights into the regulatory function of the CTTs in kinesin-microtubule binding process, which may facilitate the development of therapeutic strategies targeting CTTs-mediated interactions. - Source: PubMed
Publication date: 2026/05/21
Shen TingLi YuyanLi YangleZhao JingjingMa JianxinCheng HaojieZhang JiayiZhou MengZheng WeiHu DehuaLi LinLiu KefuSun Shengjie