EPM2A Antibody

Code CSB-PA007738ESR1HU
Size US$166
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  • Immunohistochemistry of paraffin-embedded human salivary gland tissue using CSB-PA007738ESR1HU at dilution of 1:100

  • Immunohistochemistry of paraffin-embedded human kidney tissue using CSB-PA007738ESR1HU at dilution of 1:100

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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) EPM2A Polyclonal antibody
Uniprot No.
Target Names
EPM2A
Alternative Names
Epilepsy progressive myoclonus type 2 Lafora disease (laforin) antibody; Epilepsy progressive myoclonus type 2A Lafora disease (laforin) antibody; EPM2 antibody; Epm2a antibody; Epm2a gene antibody; EPM2A_HUMAN antibody; Lafora PTPase antibody; Laforin antibody; LAFPTPase antibody; LD antibody; LDE antibody; MELF antibody; RP3-466P17.2 antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Laforin protein (244-331AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Form
Liquid
Tested Applications
ELISA, IHC
Recommended Dilution
Application Recommended Dilution
IHC 1:20-1:200
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with phosphoserine and phosphothreonine substrates (in vitro). Has been shown to dephosphorylate MAPT. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway.; does not bind to glycogen. Lacks phosphatase activity and might function as a dominant-negative regulator for the phosphatase activity of isoform 1 and isoform 7.; has phosphatase activity (in vitro).
Gene References into Functions
  1. rs702304 and rs2235481 within the EPM2A gene were associated with schizophrenia liability. PMID: 27092952
  2. Laforin prevents the auto-degradation of malin by presenting itself as a substrate. Malin preferentially degrades the phosphatase-inactive laforin monomer. PMID: 26648032
  3. Laforin-glycan interactions occur with a favourable enthalpic contribution counter-balanced by an unfavourable entropic contribution. PMID: 26578817
  4. laforin is responsible for glycogen dephosphorylation during exercise and acts during the cytosolic degradation of glycogen PMID: 26216881
  5. Lafora disease proteins laforin and malin negatively regulate the HIPK2-p53 cell death pathway. PMID: 26102034
  6. This study suggest that variations in phenotypes of EPM2A-deficient Lafora disease. PMID: 25246353
  7. novel molecular determinants in the laforin active site that help decipher the mechanism of glucan phosphatase activity. PMID: 25538239
  8. The crystal structure of laforin bound to phosphoglucan product, reveals its unique integrated tertiary and quaternary structure. PMID: 25544560
  9. This study identified some Mild Lafora disease have EPM2A mutation. PMID: 25270369
  10. 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. PMID: 24770803
  11. Polyglucosan body degradation requires a protein assembly that includes laforin and malin. PMID: 24068615
  12. 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. PMID: 23904258
  13. These results suggest that cysteine 329 is specifically involved in the dimerization process of laforin. PMID: 23922729
  14. A new novel mutation of the EPM2A gene is identified that causes Lafora disease. PMID: 23313408
  15. Studies indicate that laforin directly dephosphorylates glycogen. PMID: 22364389
  16. 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) PMID: 22815132
  17. This study identified that EPM2 gene mutations leading to Lafora disease in six Turkish families. PMID: 22047982
  18. alternative splicing could possibly be one of the mechanisms by which EPM2A may regulate the cellular functions of the proteins it codes for PMID: 22036712
  19. Genetic analysis showed a novel c.659 T>A mutation on exon 3 of the EPM2A gene, in a patient with Lafora's disease. PMID: 21371719
  20. laforin monomer is the dominant form of the protein and that it contains phosphatase activity. PMID: 21887368
  21. Laforin and malin are defective in Lafora disease (LD), a neurodegenerative disorder associated with epileptic seizures PMID: 21652633
  22. glycogen phosphorylation can be considered a catalytic error and laforin a repair enzyme. PMID: 21930129
  23. results of the present study suggest that phosphorylation of laforin-Ser(25) by AMPK provides a mechanism to modulate the interaction between laforin and malin PMID: 21728993
  24. study described several novel mutations of EPM2A and NHLRC1 and brought additional data to genetic epidemiology of Lafora disease (LD); emphasized the high mutation rate in patients with classical LD as well as the high negativity rate of skin biopsy PMID: 20738377
  25. These results suggest that the modification introduced by the laforin-malin complex could affect the subcellular distribution of AMPK beta subunits. PMID: 20534808
  26. Laforin regulates autophagy. PMID: 20453062
  27. Laforin is an active phosphatase; therefore, isoforms targeted to different cellular compartments might dephosphorylate and regulate distinct cellular substrates. PMID: 11883934
  28. identification of mutations in EPM2A with phenotypes of 22 patients (14 families) and identification of two subsyndromes PMID: 12019207
  29. The EPM2AIP1 gene was identified and characterized in a screen for laforin-interacting proteins with a human brain cDNA library; the specificity of the interaction was confirmed; subcellular colocalization of laforin and EPM2AIP1 protein was demonstrated PMID: 12782127
  30. Laforin interacts with HIRPI5. PMID: 12915448
  31. Up to 20% cases of LD are not genetically linked to chromosome 6. We report two sisters affected from bioptically diagnosed LD but without evidence of EPM2A mutation PMID: 14643920
  32. encodes a 331 amino acid protein that contains an N-terminal carbohydrate-binding domain (CBD) and a C-terminal dual-specificity phosphatase domain. The CBD of laforin targets the protein to Lafora inclusion bodies. PMID: 14706656
  33. Six novel mutations were identified, one of which is the first mutation specific to the cytoplasmic laforin isoform, implicating this isoform in disease pathogenesis. PMID: 14722920
  34. Laforin is a Glycogen-Synthase-Kinase-3 Ser 9 phosphatase, and therefore capable of inactivating GS through GSK3. PMID: 16115820
  35. Laforin does not dephosphorylate GSK3B (beta) in vitro, but possesses the unique ability to utilize a phosphorylated complex carbohydrate as a substrate and this function may be necessary for the maintenance of normal cellular glycogen. PMID: 16901901
  36. Inactivation of Epm2a resulted in increased Wnt signaling and tumorigenesis PMID: 16959610
  37. 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 PMID: 16971387
  38. Defects in laforin may lead to increased levels of misfolded and/or target proteins, which may eventually affect the physiological processes of the neuron, and likely to be the primary trigger in the physiopathology of lafora disease. PMID: 17337485
  39. study concludse that considerable variability in the age at onset of Lafora disease can occur within families; identical mutations can be associated with the classic adolescent presentation, as well as late-onset cases PMID: 17509003
  40. Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway. PMID: 18029386
  41. Results suggest that the altered subcellular localization of mutant proteins of the EPM2A and NHLRC1 genes could be one of the molecular bases of the Lafora disease phenotype. PMID: 18311786
  42. EPM2A regulated by alternative splicing plays roles in Lafora progressive myoclonus epilepsy. PMID: 18617530
  43. Laforin and malin interact with misfolded proteins and promote their degradation through the ubiquitin-proteasome system. PMID: 19036738
  44. phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity. PMID: 19171932
  45. Mutations of EPM2A formed aggregates and elicited endoplasm reticulum stress in neuronal cell. PMID: 19403557
  46. laforin and malin play a role protecting cells from ER-stress, likely contributing to the elimination of unfolded proteins PMID: 19529779
  47. Laforin is conserved in all vertebrates and a small class of protists; it is not found in other organisms. Additionally, laforin is a functional equivalent of the plant phosphatase SEX4, and it may function to dephosphorylate complex carbohydrates. PMID: 17646401
  48. Laforin acts as a scaffold that allows the E3 ubiquitin ligase malin to ubiquitinate protein targeting to glycogen (PTG). These results suggest an additional mechanism, involving laforin and malin, in regulating glycogen metabolism. PMID: 18070875

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Involvement in disease
Epilepsy, progressive myoclonic 2 (EPM2)
Subcellular Location
Cytoplasm.; [Isoform 1]: Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane.; [Isoform 2]: Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane. Nucleus.; [Isoform 4]: Cytoplasm. Nucleus.; [Isoform 5]: Cytoplasm. Nucleus.; [Isoform 7]: Cytoplasm.
Protein Families
Protein-tyrosine phosphatase family
Tissue Specificity
Expressed in heart, skeletal muscle, kidney, pancreas and brain. Isoform 4 is also expressed in the placenta.
Database Links

HGNC: 3413

OMIM: 254780

KEGG: hsa:7957

STRING: 9606.ENSP00000356489

UniGene: Hs.486696

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