LMNA Antibody
- Known as:
- LMNA Antibody
- Catalog number:
- XW-7335
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- LMNA Antibody
Related genes to: LMNA Antibody
- Gene:
- LMNA NIH gene
- Name:
- lamin A/C
- Previous symbol:
- LMN1, CMD1A, LGMD1B, PRO1, LMNL1
- Synonyms:
- HGPS, MADA
- Chromosome:
- 1q22
- Locus Type:
- gene with protein product
- Date approved:
- 1992-04-09
- Date modifiied:
- 2019-04-23
Related products to: LMNA Antibody
Related articles to: LMNA Antibody
- Hutchinson Gilford progeria syndrome (HGPS) is a fatal premature aging disorder caused by pathogenic farnesylated lamin A variants that disrupt nuclear architecture and DNA repair. Current therapies, including farnesyltransferase inhibitors, provide only modest survival benefits and lack molecular specificity, while mutation-specific genome-editing strategies cannot address atypical laminopathies. Here, we develop Farnesylation Amino acid Targeted Editing (FATE), a mutation-agnostic base-editing platform that selectively disrupts the LMNA farnesylation motif without affecting other farnesylated proteins. Using isogenic human pluripotent stem cell derived neuromuscular organoids (NMOs), we reveal muscle-specific progerin accumulation that sequesters 53BP1 and abolishes DNA damage foci formation. FATE eliminates perinuclear progerin, restores 53BP1 mobility, reconstitutes DNA repair foci, and normalizes heterochromatin architecture. Importantly, transient delivery of FATE mRNA conjugated with lipid nanoparticles to HGPS NMOs achieves efficient base editing and phenotypic rescue. These findings establish FATE as a mutation-independent therapeutic strategy targeting a fundamental pathogenic mechanism in HGPS and provide a proof-of-concept for RNA-based in situ genome editing in progeroid disease. - Source: PubMed
Publication date: 2026/08/31
Kim Dong-WooKwon Eun-JiJeon Beom-JinKwon Dong-HyeokJang GooYoon YoungyoonHwang YunaLee HyukjinCha Hyuk-Jin - Atrial standstill (AS) is the complete absence of atrial electrical and mechanical activity caused by diffuse atrial myocardial disease, distinct from sinus node dysfunction. First documented in 1897 and often misdiagnosed as atrial fibrillation, it arises from SCN5A loss-of-function, NPPA, or EMD/LMNA mutations, muscular dystrophies, and infiltrative or idiopathic fibrotic processes. Diagnosis requires absent P waves, absent atrial electrograms, and failure of atrial capture at maximal pacing output, with late gadolinium enhancement MRI and electroanatomic mapping demonstrating diffuse fibrosis. Thromboembolism complicates 30-54% of cases. Management comprises permanent pacing, anticoagulation, and gene-specific risk stratification for defibrillator eligibility. AS is best understood as the end-stage of fibrotic atrial cardiomyopathy (EHRAS Class II-III); absence of trials, unvalidated risk tools, and incomplete genotype-phenotype correlation warrant a multicenter registry. - Source: PubMed
Publication date: 2026/09/30
Lin MinDeng XiaoqiXia YuYang YongLi HairuiMeng XiangbinDing LigangLi Haiying - - Source: PubMed
Publication date: 2026/09/29
Dymek JakubJurecki SebastianOrszulak MichałPolak KarolinaHoffmann AndrzejSwinarew AndrzejMizia-Stec Katarzyna - Mutations in the gene encoding A-type lamins cause multiple muscular dystrophies (-MD). Lamins are intermediate filaments with three conserved domains: an N-terminal head, a coiled-coil rod, and a C-terminal domain possessing an Ig-like fold. Missense mutations in all three domains can cause -MD by mechanisms that are not well understood. Currently, there are limited treatments for -MD beyond symptom management. In this study, our goal was to identify candidate treatments through an in vivo drug repurposing screen using Drosophila models of -MD that recapitulate aspects of the disease phenotype. Expression of R264Q (Drosophila orthologue of human R249Q) in fly muscles causes muscle defects and premature death. We fed 1520, mostly FDA/EMA-approved, drugs to larvae and screened for rescue of lethality. This screen resulted in 68 positive hit drugs that partially restored viability. Molecular fingerprinting clustered a subset of these compounds into six structurally related groups, including L-type voltage-gated calcium channel inhibitors. We tested these inhibitors using multiple fly models expressing different mutant lamins and discovered that only flies expressing amino acid substitutions in the rod domain benefited, supporting a need for personalized treatments. Collectively, our findings support L-type voltage-gated calcium channel blockers as candidate treatments that warrant testing in pre-clinical models. - Source: PubMed
Publication date: 2026/09/19
Mohar Nathaniel PPowers Brenna AHinz Benjamin EBock Alex RMcCoy-Munger HaileyDarr ZacharyShumaker Maxwell WWemmie Alexander TSaxena AmyaWallrath Lori L - Mutations in the gene, which encodes the nuclear envelope proteins lamins A and C, account for 6% to 8% of all cases of congenital dilated cardiomyopathy. -related dilated cardiomyopathy is among the most severe forms of dilated cardiomyopathy, with limited treatment options due to an incomplete understanding of its molecular mechanisms. - Source: PubMed
Publication date: 2026/09/25
Zuela-Sopilniak NoamMorival Julien L PNtekas IoannisElpers Margaret AAgarwal RohitHenretta Sarah JOdell Jacob DDe Vlaminck IwijnLammerding Jan