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EPM2A encodes a dual-specificity phosphatase that associates with polyribosomes. Additionally we are shipping EPM2A Proteins (7) and EPM2A Kits (4) and many more products for this protein.
Showing 10 out of 162 products:
Human Monoclonal EPM2A Primary Antibody for EIA, WB - ABIN336090
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 3 references for ABIN336090
Human Polyclonal EPM2A Primary Antibody for EIA, IHC (p) - ABIN356954
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 references for ABIN356954
Human Polyclonal EPM2A Primary Antibody for EIA, WB - ABIN1449985
Worby, Gentry, Dixon: Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. in The Journal of biological chemistry 2006
Show all 2 references for ABIN1449985
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
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
This study also suggests a malin (show NHLRC1 Antibodies) function independent of laforin, possibly in lysosomal biogenesis and/or lysosomal glycogen (show GYS1 Antibodies) 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 (show INS Antibodies) sensitivity.
malin (show NHLRC1 Antibodies) functions to regulate laforin and that malin (show NHLRC1 Antibodies) deficiency at least in part causes LB and LD through increased laforin binding to glycogen (show GYS1 Antibodies).
Results show that a functional laforin-malin (show NHLRC1 Antibodies) 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 (show INS Antibodies) sensitivity.
Laforin prevents the auto-degradation of malin (show NHLRC1 Antibodies) by presenting itself as a substrate. Malin (show NHLRC1 Antibodies) 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 (show GYS1 Antibodies) dephosphorylation during exercise and acts during the cytosolic degradation of glycogen (show GYS1 Antibodies)
Lafora disease proteins laforin and malin (show NHLRC1 Antibodies) negatively regulate the HIPK2 (show HIPK2 Antibodies)-p53 (show TP53 Antibodies) 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 (show GYS1 Antibodies) binding.
Polyglucosan body degradation requires a protein assembly that includes laforin and malin (show NHLRC1 Antibodies).
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)