EPM2AIP1 Antibody (YS-62): sc-100651

EPM2AIP1 Antibody (YS-62) is a mouse monoclonal IgG2b kappa light chain antibody that detects EPM2AIP1 of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-EPM2AIP1 antibody (YS-62) is available as a non-conjugated format, providing researchers with a reliable tool for studying this important protein. EPM2AIP1, also known as laforin-interacting protein, is the first identified binding partner of Laforin and plays a crucial role in understanding the pathogenesis of Progressive Myoclonic Epilepsy Type 2 (EPM2), commonly referred to as Lafora disease. This autosomal recessive disorder is characterized by severe neurological symptoms, including grand mal seizures and myoclonus, typically manifesting around the age of 15, followed by rapid cognitive decline and psychotic features, with a grim prognosis of less than 10 years post-onset. EPM2AIP1 is primarily located in the endoplasmic reticulum, where EPM2AIP1 colocalizes with Laforin, highlighting its potential role in glycogen metabolism. EPM2AIP1 contains two coiled-coil domains and is expressed in various tissues, including the heart, brain, placenta, liver, pancreas, kidney, and skeletal muscle, indicating its widespread importance in cellular functions. Understanding the interactions and functions of EPM2AIP1 is vital for unraveling the complexities of Lafora disease and developing potential therapeutic strategies.

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EPM2AIP1 Antibody (YS-62) References:

1. Identification of a novel protein interacting with laforin, the EPM2a progressive myoclonus epilepsy gene product.  |  Ianzano, L., et al. 2003. Genomics. 81: 579-87. PMID: 12782127
2. Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy.  |  Chan, EM., et al. 2004. Hum Mol Genet. 13: 1117-29. PMID: 15102711
3. Glycogen and related polysaccharides inhibit the laforin dual-specificity protein phosphatase.  |  Wang, W. and Roach, PJ. 2004. Biochem Biophys Res Commun. 325: 726-30. PMID: 15541350
4. MLH1 germline epimutations as a factor in hereditary nonpolyposis colorectal cancer.  |  Hitchins, M., et al. 2005. Gastroenterology. 129: 1392-9. PMID: 16285940
5. Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates.  |  Worby, CA., et al. 2006. J Biol Chem. 281: 30412-8. PMID: 16901901
6. Lafora disease.  |  Madhavan, D. and Kuzniecky, RI. 2006. Rev Neurol Dis. 3: 131-5. PMID: 17047580
7. Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo.  |  Tagliabracci, VS., et al. 2007. Proc Natl Acad Sci U S A. 104: 19262-6. PMID: 18040046