TBCD antibody
- Known as:
- TBCD (anti-)
- Catalog number:
- orb101795
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- TBCD antibody
Related genes to: TBCD antibody
- Gene:
- TBCD NIH gene
- Name:
- tubulin folding cofactor D
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 17q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-07-31
- Date modifiied:
- 2016-12-12
Related products to: TBCD antibody
Related articles to: TBCD antibody
- The aim of this study was to evaluate inter- and intraindividual variability in total bacterial count (TBC) in raw and extended boar semen and to identify management- and animal-related factors associated with this variability. Semen samples from 92 clinically healthy boars of different breeds and ages, housed in barns with varying bedding, ventilation and cooling systems, were examined monthly over a 13-month period. Progressive motility of diluted sperm (PMSd) was assessed by computer-assisted semen analysis (CASA) on the day of collection (D0) and after 7 days of storage at 16°C (D7). Total bacterial count in raw semen (TBCr) and diluted semen (TBCd) was quantified by flow cytometry. Bacterial counts varied markedly between and within boars. Breed, age and season had no effect on TBCr (P > 0.05). Samples collected by hand tended to have higher TBCr on D0 than those collected using the semi-automatic system (b = 3.84, P = 0.096). Semen from two of 3 b had higher TBCr than the other (b = 5.53, P = 0.004 and b = 6.42, P = 0.032). A clear reason for this has not been found. TBCd was negatively associated with PMSd on D0 (b = -0.67, P = 0.002). These results demonstrate substantial variability in bacterial counts in boar semen and indicate that specific housing conditions and bacterial load in diluted semen may be associated with sperm quality. - Source: PubMed
Publication date: 2026/07/16
Fischer AnnalenaDemattio LukasOchs Anna-ChristinaSiuda MathiasMalama EleniLautner MatthiasLeiding ClausBollwein Heinrich - Microtubules polymerize from cytoplasmic pools of soluble αβ-tubulin heterodimers that support diverse cellular functions. The tubulin cofactors, TBCC, TBCD, and TBCE and the Arl2 GTPase, form TBC-DEG assemblies that regulate the assembly of α- and β-tubulin into heterodimers and their disassembly, yet their underlying mechanisms remain incompletely understood. Here, we reconstitute the human TBC-DE and TBC-DEG assemblies from eukaryotic cells copurified with monomeric β-tubulin intermediates and determine their cryo-EM structures. The structures reveal that TBC-DEG disassembles αβ-tubulin by releasing α-tubulin through a lever arm-like rotation in TBCE coupled to major conformational change in Arl2 upon its nucleotide release, while TBCD tightly holds β-tubulin. TBCD dissociates α-tubulin by refolding the β-tubulin H10-S8 loop at its intradimer interface. The TBC-DEG-β-tubulin or TBC-DE-β-tubulin assemblies undergo extensive back-to-back dimerization mediated by β-β-tubulin homodimers, formed through their dissociated H8 helices at unoccupied intradimer interfaces. Structural comparisons demonstrate that TBCE's mechanical rotation, driven by the Arl2 GTPase cycle, either delivers α-tubulin or removes it from beneath the TBCD-bound β-tubulin and is directionally regulated by TBCC stabilizing αβ-tubulin interfaces. Our findings suggest that TBC-DEG/TBCC catalyzing heterodimerization of α-tubulin with β-tubulin may have evolved to counteract β-tubulin's intrinsic tendency to form off-pathway toxic homodimers through its exposed α-tubulin-binding intradimer interface. - Source: PubMed
Publication date: 2026/05/08
Taheri AryanAshaduzzaman MdGill VishvEskin Julian AAl-Bassam Jawdat - Tubulin-folding cofactor E (TBCE) plays a central role in tubulin heterodimer formation and disaggregation. Both TBCE biallelic and monoallelic pathogenic variants have been associated with human diseases involving endocrine and/or neurologic system. This study aimed to expand current knowledge on the neurodegenerative phenotype associated with TBCE variants, and to explore possible genotype-phenotype correlations. - Source: PubMed
Publication date: 2026/03/04
Sartorelli JacopoSgobbi PauloBattini RobertaSchifino MariapaolaTrovato RosannaCompagnucci ClaudiaLauri AntonellaTartaglia MarcoSferra AntonellaD'Amico AdeleDiodato DariaBertini EnricoNicita Francesco - Microtubules polymerize from cytoplasmic pools of soluble αβ-tubulin heterodimers that support diverse cellular functions. The tubulin cofactors, TBCC, TBCD, TBCE, and the Arl2 GTPase, form TBC-DEG assemblies that regulate αβ-tubulin assembly and disassembly from α- and β-tubulins, yet their underlying mechanisms remain incompletely understood. Here, we reconstitute the human TBC-DE and TBC-DEG assemblies from eukaryotic cells co-purified with monomeric β-tubulin intermediates and determine their cryo-EM structures. The structures reveal that TBC-DEG disassembles αβ-tubulin by releasing α-tubulin through a lever-arm-like rotation in TBCE coupled to major conformational change in Arl2 upon its nucleotide release, while TBCD tightly holds β-tubulin. TBCD dissociates α-tubulin by refolding the β-tubulin H10-S8 loop at its intradimer interface. The TBC-DEG-β-tubulin or TBC-DE-β-tubulin assemblies undergo extensive back-to-back dimerization mediated by β-β-tubulin homodimers, formed through their dissociated H8 helices at unoccupied intradimer interfaces. Structural comparisons demonstrate that the TBCE mechanical rotation, driven by the Arl2 GTPase cycle, either delivers α-tubulin or removes it from beneath the TBCD-bound β-tubulin and is directionally regulated by TBCC stabilizing αβ-tubulin interfaces. Our findings suggest that TBC-DEG/TBCC catalyzing heterodimerization of α-tubulin with β-tubulin may have evolved to counteract the β-tubulin intrinsic tendency to form off-pathway toxic homodimers through its exposed α-tubulin-binding intradimer interface. - Source: PubMed
Publication date: 2025/12/31
Taheri AryanAshaduzzaman MdGill VishvAl-Bassam Jawdat - Reis-Bücklers corneal dystrophy (RBCD; Mendelian Inheritance in Man 602082) and Thiel-Behnke corneal dystrophy (TBCD; Mendelian Inheritance in Man 608470) are clinically similar corneal dystrophies affecting Bowman's layer, caused by the TGFBI variants p.(Arg124Leu) and p.(Arg555Gln), respectively. Yet their distinct clinical courses complicate therapeutic decisions. This study aimed to compare the clinical course and surgical outcomes of genetically confirmed RBCD and TBCD. - Source: PubMed
Publication date: 2025/12/12
Mahoun ZacharyValleix SophieBourges Jean-Louis