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anti-Mouse (Murine) EPM2A Antibodies:
anti-Rat (Rattus) EPM2A Antibodies:
anti-Human EPM2A Antibodies:
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Human Monoclonal EPM2A Primary Antibody for ELISA, WB - ABIN563505
Tagliabracci, Turnbull, Wang, Girard, Zhao, Skurat, Delgado-Escueta, Minassian, Depaoli-Roach, Roach: Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. in Proceedings of the National Academy of Sciences of the United States of America 2007
Show all 8 Pubmed References
Monoclonal EPM2A Primary Antibody for ELISA, WB - ABIN533790
Ganesh, Delgado-Escueta, Suzuki, Francheschetti, Riggio, Avanzini, Rabinowicz, Bohlega, Bailey, Alonso, Rasmussen, Thomson, Ochoa, Prado, Medina, Yamakawa: Genotype-phenotype correlations for EPM2A mutations in Lafora's progressive myoclonus epilepsy: exon 1 mutations associate with an early-onset cognitive deficit subphenotype. in Human molecular genetics 2002
Show all 3 Pubmed References
Human Polyclonal EPM2A Primary Antibody for IHC (p), IHC - ABIN451649
Mittal, Dubey, Yamakawa, Ganesh: Lafora disease proteins malin and laforin are recruited to aggresomes in response to proteasomal impairment. in Human molecular genetics 2007
Human Polyclonal EPM2A Primary Antibody for IHC (p), ELISA - ABIN544066
Minassian, Lee, Herbrick, Huizenga, Soder, Mungall, Dunham, Gardner, Fong, Carpenter, Jardim, Satishchandra, Andermann, Snead, Lopes-Cendes, Tsui, Delgado-Escueta, Rouleau, Scherer: Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. in Nature genetics 1998
Show all 2 Pubmed References
Human Monoclonal EPM2A Primary Antibody for ELISA, WB - ABIN521711
Sherwood, Johnson, Delgado-Escueta, Gentry: A bioassay for Lafora disease and laforin glucan phosphatase activity. in Clinical biochemistry 2013
The present study analyzes possible inflammatory responses in the mouse lines Epm2a (-/-) (laforin knock-out) and Epm2b (-/-) (malin knock-out) with disease progression.
Laforin-silenced cells was able to induce autophagic flux, proteasomal activity and reduce the polyubiquitinated proteins by heat shock.
This study also suggests a malin function independent of laforin, possibly in lysosomal biogenesis and/or lysosomal glycogen disposal.
loss of laforin results in activation of serum/glucocorticoid-induced kinase 1 in cellular and animals models
expression of Epm2a blocks formation of Lafora bodies and restores the impairment in macroautophagy, preventing the development of Lafora bodies in Epm2a-deficient mice.
in laforin-deficient mice, stress drastically accelerates Lafora bodies accumulation and Lafora disease.
Results indicate that laforin has no effect on whole-body glucose metabolism and insulin sensitivity.
malin functions to regulate laforin and that malin deficiency at least in part causes LB and LD through increased laforin binding to glycogen.
Results show that a functional laforin-malin complex plays a critical role in disrupting Lafora bodies and relieving endoplasmic reticulum stres.
A detailed microscopic analysis of the neuropil of a Laforin-deficient (epm2a-/-) mouse model shows neurofibrillary degeneration and senile-like plaques prominent in the hippocampus and ventral pons.
Motor coordination, activity impairment, and memory deficits progressively increase with age in Epm2a deficient mice.
These results define laforin as a new regulator of insulin sensitivity.
Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice
Inactivation of Epm2a resulted in increased Wnt signaling and tumorigenesis
results demonstrate a critical role of dimerization in Laforin function and suggest an important new dimension in protein phosphatase function and in molecular pathogenesis of Lafora's disease
This study provides a molecular link between an observed biochemical property of laforin and the phenotype of a mouse model of Lafora disease.
laforin is a selective phosphatase for GSK-3beta and regulates cell cycle progression by GSK-3beta-dependent mechanisms and represses cyclin D1 expression
laforin functions to suppress excessive glycogen phosphorylation and is an essential component of the metabolism of normally structured glycogen, as shown in a mouse model
laforin and malin play a role protecting cells from ER-stress, likely contributing to the elimination of unfolded proteins
Study suggests that laforin is one of the critical regulators of Tau protein, that the NFTs could underlie some of the symptoms seen in Lafora disease.
rs702304 and rs2235481 within the EPM2A gene were associated with schizophrenia liability.
Laforin prevents the auto-degradation of malin by presenting itself as a substrate. Malin preferentially degrades the phosphatase-inactive laforin monomer.
Laforin-glycan interactions occur with a favourable enthalpic contribution counter-balanced by an unfavourable entropic contribution.
laforin is responsible for glycogen dephosphorylation during exercise and acts during the cytosolic degradation of glycogen
Lafora disease proteins laforin and malin negatively regulate the HIPK2-p53 cell death pathway.
This study suggest that variations in phenotypes of EPM2A-deficient Lafora disease.
novel molecular determinants in the laforin active site that help decipher the mechanism of glucan phosphatase activity.
The crystal structure of laforin bound to phosphoglucan product, reveals its unique integrated tertiary and quaternary structure.
This study identified some Mild Lafora disease have EPM2A mutation.
Studied the role of conformational changes in human laforin structure due to existing single mutation W32G and prepared double mutation W32G/K87A related to loss of glycogen binding.
Polyglucosan body degradation requires a protein assembly that includes laforin and malin.
This study identified the flexibility of K87A mutated laforin structure, with replacement of acidic amino acid to aliphatic amino acid in functional carbohydrate binding module domain, have more impact in abolishing glycogen binding that favors Lafora disease.
These results suggest that cysteine 329 is specifically involved in the dimerization process of laforin.
A new novel mutation of the EPM2A gene is identified that causes Lafora disease.
Studies indicate that laforin directly dephosphorylates glycogen.
Malin forms a functional complex with laforin. This complex promotes the ubiquitination of proteins involved in glycogen metabolism and misregulation of pathways involved in this process results in Lafora body formation. (Review)
This study identified that EPM2 gene mutations leading to Lafora disease in six Turkish families.
alternative splicing could possibly be one of the mechanisms by which EPM2A may regulate the cellular functions of the proteins it codes for
Genetic analysis showed a novel c.659 T>A mutation on exon 3 of the EPM2A gene, in a patient with Lafora's disease.
laforin monomer is the dominant form of the protein and that it contains phosphatase activity.
This gene encodes a dual-specificity phosphatase that associates with polyribosomes. The encoded protein may be involved in the regulation of glycogen metabolism. Mutations in this gene have been associated with myoclonic epilepsy of Lafora. Alternative splicing results in multiple transcript variants.
, lafora PTPase
, epilepsy, progressive myoclonic epilepsy, type 2 gene alpha
, epilepsy, progressive myoclonus type 2, Lafora disease (laforin)