Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
EPM2A encodes a dual-specificity phosphatase that associates with polyribosomes. Additionally we are shipping EPM2A Antibodies (163) and EPM2A Kits (4) and many more products for this protein.
Showing 5 out of 7 products:
This study also suggests a malin (show NHLRC1 Proteins) function independent of laforin, possibly in lysosomal biogenesis and/or lysosomal glycogen (show GYS1 Proteins) 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 Proteins) sensitivity.
malin (show NHLRC1 Proteins) functions to regulate laforin and that malin (show NHLRC1 Proteins) deficiency at least in part causes LB and LD through increased laforin binding to glycogen (show GYS1 Proteins).
Results show that a functional laforin-malin (show NHLRC1 Proteins) 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 Proteins) sensitivity.
rs702304 and rs2235481 within the EPM2A gene were associated with schizophrenia liability.
Laforin prevents the auto-degradation of malin (show NHLRC1 Proteins) by presenting itself as a substrate. Malin (show NHLRC1 Proteins) 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 Proteins) dephosphorylation during exercise and acts during the cytosolic degradation of glycogen (show GYS1 Proteins)
Lafora disease proteins laforin and malin (show NHLRC1 Proteins) negatively regulate the HIPK2 (show HIPK2 Proteins)-p53 (show TP53 Proteins) 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 Proteins) binding.
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)