• NatureSynthetic
  • Amino Acid Sequence
    • SpeciesHuman
    • SequenceKFGKVRSSVCSL
    • Amino acids320 to 331


Our Abpromise guarantee covers the use of ab45659 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications


  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

General Info

  • Alternative names
    • Epilepsy progressive myoclonus type 2 Lafora disease (laforin)
    • Epilepsy progressive myoclonus type 2A Lafora disease (laforin)
    • EPM2
    • Epm2a
    • Epm2a gene
    • Lafora PTPase
    • Laforin
    • LAFPTPase
    • LD
    • LDE
    • MELF
    • RP3-466P17.2
    see all
  • FunctionDual specificity protein phosphatase. May be involved in the control of glycogen metabolism, particularly in monitoring for and preventing the formation of poorly branched glycogen molecules (polyglucosans). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Forms a complex with NHLRC1/malin and HSP70 and this complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1.
  • Tissue specificityExpressed in heart, skeletal muscle, kidney, pancreas and brain. Isoform 4 is also expressed in the placenta.
  • Involvement in diseaseDefects in EPM2A are a cause of progressive myoclonic epilepsy type 2 (EPM2) [MIM:254780]; also known as Lafora disease. EPM2 is an autosomal recessive and severe form of adolescent-onset progressive epilepsy. Typically, as seizures increase in frequency, cognitive function declines towards dementia, and affected individuals die usually within 10 years after onset. EPM2 occurs worldwide, but it is particularly common in the mediterranean countries of southern Europe and northern Africa, in southern India and in the Middle East. At the cellular level, it is characterized by accumulation of starch-like polyglucosans called Lafora bodies (LBs) that are most abundant in organs with the highest glucose metabolism: brain, heart, liver and skeletal muscle. Among other conditions involving polyglucosans, EPM2 is unique in that the inclusions are in neuronal dendrites but not axons and the forming polyglucosan fibrils are associated with the endoplasmic reticulum.
  • Sequence similaritiesBelongs to the protein-tyrosine phosphatase family.
    Contains 1 CBM20 (carbohydrate binding type-20) domain.
    Contains 1 tyrosine-protein phosphatase domain.
  • Post-translational
    Polyubiquitinated by NHLRC1/malin.
    Phosphorylation on Ser-25 by AMPK affects the phosphatase activity of the enzyme and its ability to homodimerize and interact with NHLRC1, PPP1R3C or PRKAA2.
  • Cellular localizationCytoplasm; Cytoplasm. Nucleus; Endoplasmic reticulum. Cell membrane. Nucleus. Also found in the nucleus; Endoplasmic reticulum. Cell membrane. Primarily associated with polyribosomes at the endoplasmic reticulum, also found at the plasma membrane and Cytoplasm. Under glycogenolytic conditions localizes to the nucleus.
  • Information by UniProt

References for EPM2A peptide (320-331) (ab45659)

ab45659 has not yet been referenced specifically in any publications.

Product Wall

There are currently no Abreviews or Questions for ab45659.
Please use the links above to contact us or submit feedback about this product.