|Application ||WB, IHC, E|
|Other Accession||NP_005661, 7957, 13853 (mouse), 680683 (rat)|
|Predicted||Mouse, Rat, Dog, Cow|
|Calculated MW||37158 Da|
|Other Names||Laforin, 3.1.3.-, 184.108.40.206, 220.127.116.11, Glucan phosphatase, Lafora PTPase, LAFPTPase, EPM2A|
|Format||0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Goat Anti-Laforin (isoform a) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Has both dual-specificity protein phosphatase and glucan phosphatase activities. Together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. 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. Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1.|
|Cellular Location||Cytoplasm Note=Under glycogenolytic conditions localizes to the nucleus Isoform 2: Endoplasmic reticulum. Cell membrane. Nucleus. Note=Also found in the nucleus Isoform 5: Cytoplasm. Nucleus.|
|Tissue Location||Expressed in heart, skeletal muscle, kidney, pancreas and brain. Isoform 4 is also expressed in the placenta|
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Provided below are standard protocols that you may find useful for product applications.
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.
Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin. Vernia S, et al. PLoS One, 2009 Jun 16. PMID 19529779.
Deletions and missense mutations of EPM2A exacerbate unfolded protein response and apoptosis of neuronal cells induced by endoplasm reticulum stress. Liu Y, et al. Hum Mol Genet, 2009 Jul 15. PMID 19403557.
Lafora progressive myoclonus epilepsy: a meta-analysis of reported mutations in the first decade following the discovery of the EPM2A and NHLRC1 genes. Singh S, et al. Hum Mutat, 2009 May. PMID 19267391.
AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex. Vernia S, et al. J Biol Chem, 2009 Mar 27. PMID 19171932.
The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Garyali P, et al. Hum Mol Genet, 2009 Feb 15. PMID 19036738.
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