BBS9
- Known as:
- BBS9
- Catalog number:
- 002441A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- BBS9
Related genes to: BBS9
- Gene:
- BBS9 NIH gene
- Name:
- Bardet-Biedl syndrome 9
- Previous symbol:
- -
- Synonyms:
- B1, PTHB1
- Chromosome:
- 7p14.3
- Locus Type:
- gene with protein product
- Date approved:
- 2007-01-18
- Date modifiied:
- 2016-10-05
Related products to: BBS9
anti-BBS9anti-BBS9anti-BBS9 type: Primary antibodies host: RabbitBardet-Biedl syndrome 9 protein homolog,Bbs9,Mouse,Mus musculus,Parathyroid hormone-responsive B1 gene protein homolog,Protein PTHB1,Pthb1Bardet-Biedl syndrome 9 protein,BBS9,Homo sapiens,Human,Parathyroid hormone-responsive B1 gene protein,Protein PTHB1,PTHB1BBS5 Gene Bardet-Biedl syndrome 5BBS9 / PTHB1 antibody Host RabbitBBS9 3&_39;UTR Lenti-reporter-Luc VectorBBS9 Antibody - N-terminal region (ARP65858_P050)BBS9 Gene Bardet-Biedl syndrome 9BBS9 Over-expression Lysate ProductBBS9 Polyclonal Antibody, ALEXA FLUOR 594 ConjugatedBBS9 Primary Antibody, BBS9, Species: Human Recombinant Protein Source: Rabbit PolyclonalBBS9 purified MaxPab rabbit polyclonal antibody (D02P)BBS9 siRNA_Lentivectors Related articles to: BBS9
- Eukaryotic flagella are evolutionarily conserved organelles that mediate motility, sensory transduction, and environmental adaptation, yet their presence and gene composition vary considerably across algal lineages. Dinoflagellates, a lineage within the superphylum Alveolata, derived from secondary endosymbiosis, exhibit larger and more reorganized genomes than their red-algal relatives and possess a distinctive biflagellate morphology, making them an informative group for studying flagellar evolution. To systematically investigate flagellar gene distribution in this lineage, we performed comparative genomic analyses on 102 genomes spanning four algal groups-Chlorophyta, Rhodophyta, Alveolata (represented by dinoflagellates), and Bacillariophyta. Genomes were selected based on assembly completeness, retaining only those with BUSCO completeness > 50% to balance data quality with taxonomic coverage. Orthologous groups were identified using a reciprocal best BLAST v2.11.0(rBH) strategy, from which we curated 94 conserved flagellar gene families. Quantitative comparisons revealed significant lineage-specific expansions of flagellar gene families within dinoflagellates, including , , and , with fold enrichment values ranging from 3.6 to 5.8 (adjusted < 0.01). Phylogenetic analyses further identified two axonemal components, and , as candidates acquired via horizontal gene transfer, with bootstrap support exceeding 80% and Alien Index values > 45. Collectively, these phylogenomic analyses suggest that lineage-specific expansion and horizontal gene transfer have jointly contributed to the evolution of flagellar systems in dinoflagellates, providing a framework for future functional studies. - Source: PubMed
Publication date: 2026/07/02
Jia LiminHou YinguangZhang ManLi LiangweiZhang YaoleiWang JiahaoYuan ZengbaoFan GuangyiShi ChengchengZhao Hansheng - The BBSome, an eight-protein complex implicated in Bardet-Biedl syndrome (BBS), plays a crucial role in various cellular processes including ciliary function. Although important aspects of its structural organization and protein interactions have been elucidated, additional questions remain regarding how these features relate to cargo recognition and complex dynamics. Using AlphaFold3, we generated a structural model closely matching recent cryo-EM data (α-carbon root means square deviation: 1.203 Å). Interface residue analysis of the model identified BBSome proteins BBS1 and BBS9 as central interaction hubs (most interface residues between two proteins), with BBS2 and BBS7 showing the most polar contacts. The common BBS1 pathogenic mutation, known to cause BBS, was predicted to destabilize the complex. BBS4 was also found to interact stably with pericentriolar material 1, suggesting a role in centriolar satellite localization. AlphaFold3-mediated analysis of BBSome interactions with G protein-coupled receptors (GPCRs) led to the identification of contact hotspots on BBS1, BBS4, and BBS5. These predictions were supported by immunoprecipitation and peptide competition assays. The modeling also suggested plausible interfaces between specific BBS proteins and metabolic signaling proteins, including melanocortin receptor accessory protein 2 (MRAP2) [an melanocortin-4 receptor (MC4R) chaperonin], the leptin receptor, and the insulin receptor. These predicted interfaces align with previously reported biochemical associations between BBS proteins and these receptors, supporting the idea that the BBSome regulates trafficking and signaling in metabolic pathways. Together, these findings provide new insights into BBSome structure and receptor interactions, offering a predictive framework to explore its role in ciliary trafficking and human disease. This study combines AI modeling and experimental validation to define key structural features and receptor interactions of the BBSome complex. The analysis identifies BBS1 and BBS9 as central hubs, reveals how the BBS1 mutation destabilizes the complex, and uncovers novel contacts with various receptors including those involved in metabolic regulation. These findings provide a predictive framework linking BBSome structure to ciliary signaling and metabolic regulation in Bardet-Biedl syndrome. - Source: PubMed
Publication date: 2026/03/31
Guo Deng FuRouabhi YounesTollefson MalloryVorhies KaiRahmouni Kamal - Bardet-Biedl syndrome (BBS) is a rare autosomal recessive ciliopathy with multisystem involvement. While BBS1 mutations are common globally, population-specific genetic patterns and phenotype severity vary. This study aimed to investigate genotype-phenotype correlations in an Indian cohort. - Source: PubMed
Publication date: 2026/03/01
Thiriveedi DeepakGoroshi ManjunathGanakumar VanishriGhatnatti Vikrant - This case describes the resolution of refractory chronic idiopathic urticaria (CIU) with setmelanotide in a patient with Bardet-Biedl Syndrome (BBS). While setmelanotide is approved for syndromic obesity, this report highlights a novel anti-inflammatory effect potentially mediated by melanocortin-4 receptor (MC4R) agonism, expanding current understanding of its immunomodulatory role in mast cell-mediated disease. - Source: PubMed
Publication date: 2025/11/03
Haggerty KateBlack JenniferAbeles Ruth - To investigate the relationship between peripheral blood circular RNA Bardet-Biedl syndrome 9 (circBBS9) and circRNA catenin beta 1 (circCTNNB1) and weaning failure of mechanical ventilation in patients with acute exacerbation of chronic obstructive pulmonary disease (AECOPD). - Source: PubMed
Guo ZhiqiangLiu YunfengTan JunhuiYang BowenJiao Jiao