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anti-Human Lamin A/C Antibodies:
anti-Mouse (Murine) Lamin A/C Antibodies:
anti-Rat (Rattus) Lamin A/C Antibodies:
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Human Polyclonal Lamin A/C Primary Antibody for IHC, WB - ABIN6672084
Ye, Jiang, Cui, Zhu, Sun, Wang, Zohaib, Dong, Ruan, Song, He, Chen, Cao: Etanercept reduces neuroinflammation and lethality in mouse model of Japanese encephalitis. in The Journal of infectious diseases 2014
Show all 11 Pubmed References
Mouse (Murine) Polyclonal Lamin A/C Primary Antibody for IHC, WB - ABIN3020785
Wei, Dai, Zhou, He, Yao, Zhao, Guo, Yang: Oroxylin A activates PKM1/HNF4 alpha to induce hepatoma differentiation and block cancer progression. in Cell death & disease 2018
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Human Monoclonal Lamin A/C Primary Antibody for ICC, FACS - ABIN335389
Broers, Machiels, Kuijpers, Smedts, van den Kieboom, Raymond, Ramaekers: A- and B-type lamins are differentially expressed in normal human tissues. in Histochemistry and cell biology 1997
Show all 10 Pubmed References
Green monkey (Chlorocebus) Monoclonal Lamin A/C Primary Antibody for ICC, FACS - ABIN303591
Vaughan, Alvarez-Reyes, Bridger, Broers, Ramaekers, Wehnert, Morris, Whitfield WGF, Hutchison: Both emerin and lamin C depend on lamin A for localization at the nuclear envelope. in Journal of cell science 2001
Show all 8 Pubmed References
Human Polyclonal Lamin A/C Primary Antibody for IF, IHC - ABIN6712003
Chen, Wang, Lu, Zhang, Fu, Luo: Cholesterol sequestration by nystatin enhances the uptake and activity of endostatin in endothelium via regulating distinct endocytic pathways. in Blood 2011
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Human Polyclonal Lamin A/C Primary Antibody for FACS, ICC - ABIN4330008
Kiel, Busch, Meyer-Rachner, Hübner: Laminopathy-inducing mutations reduce nuclear import of expressed prelamin A. in The international journal of biochemistry & cell biology 2014
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Human Polyclonal Lamin A/C Primary Antibody for ICC, IHC (p) - ABIN3043695
Liu, Ma, Wu, Li, Zhang, Han, Wang, Reindl, Wu, Ma: Arginine deiminase augments the chemosensitivity of argininosuccinate synthetase-deficient pancreatic cancer cells to gemcitabine via inhibition of NF-?B signaling. in BMC cancer 2014
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Human Monoclonal Lamin A/C Primary Antibody for ICC, FACS - ABIN335390
Neri, Raymond, Giordano, Borgatti, Marchisio, Capitani, Martelli: Spatial distribution of lamin A and B1 in the K562 cell nuclear matrix stabilized with metal ions. in Journal of cellular biochemistry 1999
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Human Polyclonal Lamin A/C Primary Antibody for WB - ABIN537492
Lei, Liu, Sodja, LeBlanc, Ribecco-Lutkiewicz, Smith, Charlebois, Walker, Sikorska: S/MAR-binding properties of Sox2 and its involvement in apoptosis of human NT2 neural precursors. in Cell death and differentiation 2005
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Human Polyclonal Lamin A/C Primary Antibody for ICC, IHC (p) - ABIN3043295
Yang, Liu, Zhu, Zhang, Xi, Hu, He, Jiang: Human peripheral nerve-derived scaffold for tissue-engineered nerve grafts: histology and biocompatibility analysis. in Journal of biomedical materials research. Part B, Applied biomaterials 2010
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5' splice site selection in LMNA is determined by an intricate interplay among RNA sequence, secondary structure and splice site position
LMNA Mutation Leads to Aberrant Dentin Formation.
the effect of a LMNA mutation is strongly dependent not only on a specific mutation itself, but also might be influenced by the intrinsic molecular context of a cell lineage.
Nuclear Nox4 interaction with prelamin A is associated with nuclear redox control of mesnechymal stem cell aging.
Lamin A/C expression was primarily localized in the nuclear envelope of intervertebral disc degeneration cells, and associated with apoptosis in cell nuclei
Together these systems offer powerful methodology to study ZMPSTE24 disease alleles and to dissect the specific residues and features of the lamin A tail that are required for recognition and cleavage by the ZMPSTE24 protease.
Several cardiac phenotypes were age-dependently increased in LMNA mutation carriers, suggesting that ICD or CRT-D could suppress SCD after middle age; however, LVD leading to end-stage heart failure was the only independent predictor for total mortality.
Study reveals that three flexible linker regions in the lamin A coiled coil rod can electrostatically drive sliding of adjacent coiled coil segments onto each other to achieve a spring-like contraction in rod length. Both head and tail unstructured regions flanking the rod can act as dynamic polar bridges stabilising the lamin A tetrameric interface and likely defining their assembly dynamics.
These observations suggest that sufficient pools of telomeres and a nuclear lamin A component contribute to the cellular robustness against DNA damage induced by therapeutic treatment in human cancer cells.
Skeletal Muscle Dystrophy mutant of lamin A alters the structure and dynamics of the Ig fold domain.
this study shows that vascular smooth muscle-specific progerin expression accelerates atherosclerosis and death in a mouse model of Hutchinson-Gilford Progeria syndrome
Identify a large family, spanning five generations, with the novel LMNA nonsense mutation c.544C>T in exon 3 resulting in familial cardiomyopathy with a severe arrhythmogenic phenotype, and sudden cardiac death.
The LMNA-associated lipodystrophic features, combining generalized or partial fat atrophy and metabolic alterations associated with insulin resistance, could result from altered adipocyte differentiation or from altered fat structure.
REVIEW: findings presented here collectively argue towards a deregulation of large-scale and local spatial genome organization by a subset of lamin A mutations causing laminopathies.
Hutchinson-Gilford progeria cells show impaired lamin A/C-HDAC2 interplay and accumulation of p21 upon stress recovery.
Lamin A/C E161K, D192G, and N195K mutations generate distinctive structural changes correlated with clinical phenotype severity.
Premature cardiac death and aging is the hallmark of Hutchinson-Gilford syndrome, a disease caused by defined mutations in the lamin A gene leading to a shortened prelamin A protein known as progerin. The here presented data suggest that Body-Mass-Index strongly correlates with progerin mRNA expression and inflammation. Progerin might contribute to well described accelerated biologic aging in obese individuals.
The expression levels of the Lamin A/C transcript variants were measured in samples derived from MCF7 and U937 cell lines. RT-qPCR assay was also used to quantitate and compare the mRNA expression of splice variants of Lamin A/C.
This study has concluded that Identification of culprit mutations within SCN5A and LMNA provides further insight into the pathophysiology underlying the condition and emphasizes a potential role for routine clinical genetic testing for idiopathic BBRVT.
The results highlighted a global perturbation of transcripts derived from repetitive sequences in a cellular model of aging and provided a direct link between progerin expression and alteration of transcription from human repetitive elements.
Depletion of Lamin A-C and Lap2alpha reduces 53BP1 accumulation at UV-induced DNA lesions.
This study reveals mechanisms underlying progerin toxicity, including replication stress-induced genomic instability and activation of IFN-like responses.
mouse lamin A dC50 cDNA encoding progerin that lacks 50 amino acid residues at C-terminus depresses osteoblast differentiation in both early and late stages, and it negatively regulates beta-catenin activity interacting with GSK-3beta in cytoplasm.
We showed here that NAD+ salvage pathway was altered in the heart of mouse and human carrying LMNA mutation, leading to an alteration of one of NAD+ co-substrate enzymes, PARP-1
Lamin A/C mediates Th1 polarization by a mechanism involving T-bet and IFNgamma production as key regulator of Th1 differentiation in response to viral and intracellular parasite infections.
Collectively, our novel results provide therapeutic insights into LMNA cardiomyopathy
we show that the H222P amino acid substitution in lamin A enhances its binding to ERK1/2 and increases sequestration at the nuclear envelope. Finally, we show that genetic deletion of Dusp4 has beneficial effects on heart function and prolongs survival in LmnaH222P/H222P mice. These results further establish Dusp4 as a key contributor to the pathogenesis of LMNA cardiomyopathy and a potential target for drug therapy.
Data show that lamin A/C expressing cells can form an actin cap to resist nuclear deformation in response to physiological mechanical stresses.
THE ROLE OF LMNA MUTATIONS IN MYOGENIC DIFFERENTIATION OF PRIMARY SATELLITE CELLS AND C2C12 CELLS.
Itm2a knockdown is sufficient to rescue the inhibitory effects of lamin A WT and R482W mutant overexpression on 3T3-L1 differentiation.
Using the thin film method combined with sample specific finite element modeling, we quantitatively showed a fivefold lower contractile stress generation of Lmna knockout embryonic fibroblasts (MEFs) as compared to wild-type MEFs. Via fluorescence microscopy it was demonstrated that the lower contractile stress generation was associated with an impaired actin stress fiber organization with thinner actin fibers.
Lmna gene product might play a crucial role in the ChAT-dependent molecular differentiation cascade.
Heterozygous Lmna(delK32/+) (Het) mice had similar cardiac function to wild-type (Wt) before exercise; after 5 weeks strenuous running, Het mice showed cardiac dysfunction and dilation without visible changes in cardiac morphology, molecular remodelling or nuclear structure compared to Wt exercised and Het sedentary mice. Skeletal muscle ex vivo contractile function remained unaffected in Het exercised mice.
Alterations in ventricular myocytes ion channel properties may contribute to arrhythmia and sudden cardiac death in LmnaN195K mutation-related Familial Dilated Cardiomyopathy.
our findings indicate that altered mTOR signaling in Lmna(-/-) mice leads to a lipodystrophic phenotype that can be rescued with rapamycin, highlighting the effect of loss of adipose tissue in Lmna(-/-) mice and the consequences of altered mTOR signaling
results suggest that lamin A plays important roles in maintaining the osteoblast differentiation and function
these findings show that cardiac ERK1/2 activity is modulated in part by TGF-b/Smad signaling, leading to altered activation of CTGF/CCN2 to mediate fibrosis and alter cardiac function. This identifies a novel mechanism in the development of LMNA cardiomyopathy.
Activation of WNT/b-catenin activity improved cardiac contractility and ameliorated intraventricular conduction defects in LmnaH222P/H222P mice, which was associated with increased expression of myocardial connexin 43. These results indicate that decreased WNT/b-catenin contributes to the pathophysiology of LMNA cardiomyopathy and that drugs activating b-catenin may be beneficial in affected individuals
SUMO1 conjugation of RB and Lamin A/C is modulated by the SUMO protease SENP1 and that sumoylation of both proteins is required for their interaction.
Lmna-deficient cells show a compromised strain avoidance response, which is completely abolished when topographical cues and uniaxial strain are applied along the same direction.
Study provides evidence that baculovirus infection induced lamin B phosphorylation and disruption of the nuclear lamina.
findings reveal coordination of AGO2 and LaminB function to dictate genome architecture and thereby regulate gene expression
The loss of lamin-B leads to systemic inflammation and aging.
nuclear Wash interacts with B-type Lamin (Lamin Dm0), and, like Lamin, Wash associates with constitutive heterochromatin
of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C
Rab5 associated in vivo with nuclear Lamin and mushroom body defect (Mud), the Drosophila counterpart of nuclear mitotic apparatus protein (NuMA).
Kugelkern and lamin Dm0 affect nuclear shape without requiring filament formation or the presence of a classical nuclear lamina.
Lamin mutation is associated with neuromuscular defects and premature aging.
analysis of Drosophila and human A-type lamins
prometaphase spindle can be made robust to natural fluctuations in motor ratios by a disassembling lamin-B envelope.
Null mutants of Drosophila B-type lamin Dm(0) show aberrant tissue differentiation rather than obvious nuclear shape distortion or specific defects during cell proliferation.
Molecular interactions with lamin Dm0 may link JIL-1 kinase to nuclear morphology and integrity of nurse cells during oogenesis.
The lamin Dm0 allele Ari3 acts as an enhancer of position effect variegation of the wm4 allele in Drosophila.
Both lamin Dm0 and C. elegans Ce-lamin bind directly to histone H2A in vitro and this binding requires the nuclear localization signal
Induced expression of the farnesylated lamina proteins Lamin B and Kugelkern cause aberrant nuclear shapes and reduce the lifespan of adult flies.
developmental disorders caused by lesions in the B-type lamins and interacting proteins
results have important implications for understanding the tissue-specific regulation and functions of the lamin A gene
The induction of embryonic senescence and laminopathies in zebrafish harboring disturbed expressions of the lamin A gene, is described.
These results indicate that thyroid hormone-regulated expression of nuclear lamin A and LIII closely correlates with dedifferentiation of the epithelial cells in the X. laevis intestine.
LIII filaments appear identical to the endogenous lamina, whereas lamin B2 assembles into filaments that are organized less precisely; Lamin A induces sheets of thicker filaments on the endogenous lamina and increases the rigidity of the nuclear envelope
Ectopic expression of prelamin A in early Xenopus embryos induces apoptosis.
Both anti-lamin A/C and anti-lamin B staining were clearly present in all embryonic stages.
A study mapping the location of procine lamin type A to chromosome 4q is presented.
The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. Vertebrate lamins consist of two types, A and B. Alternative splicing results in multiple transcript variants. Mutations in this gene lead to several diseases: Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.
70 kDa lamin
, lamin A/C-like 1
, renal carcinoma antigen NY-REN-32
, lamin C
, B-type lamin
, intermediate filament-like lamina
, lamin A
, lamin B
, lamin D
, lamin D[]
, lamin D[[m]]0
, lamin D[[o]]
, lamin Dm0
, lamin Dm[]
, lamin Dmo
, nuclear lamin
, lamin C2
, lamin A/C