Product Details

Purity

>85% (SDS-PAGE)

Target Names

Epm2a

Uniprot No.

Q9WUA5

Alternative Names

Epm2aLaforin; EC 3.1.3.-; EC 3.1.3.16; EC 3.1.3.48; Glucan phosphatase; Lafora PTPase; LAFPTPase

Species

Mus musculus (Mouse)

Expression Region

1-330

Target Protein Sequence

MLFRFGVVVP PAVAGARQEL LLAGSRPELG RWEPHGAVRL RPAGTAAGAA ALALQEPGLW LAEVELEAYE EAGGAEPGRV DTFWYKFLQR EPGGELHWEG NGPHHDRCCT YNEDNLVDGV YCLPVGHWIE ATGHTNEMKH TTDFYFNIAG HQAMHYSRIL PNIWLGSCPR QLEHVTIKLK HELGVTAVMN FQTEWDIIQN SSGCNRYPEP MTPDTMMKLY KEEGLSYIWM PTPDMSTEGR VQMLPQAVCL LHALLENGHT VYVHCNAGVG RSTAAVCGWL HYVIGWNLRK VQYFIMAKRP AVYIDEDALA QAQQDFSQKF GKVHSSICAL

Protein Length

full length protein

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

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. Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with 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.

Gene References into Functions

The present study analyzes possible inflammatory responses in the mouse lines Epm2a (-/-) (laforin knock-out) and Epm2b (-/-) (malin knock-out) with disease progression. PMID: 27041370
Laforin-silenced cells was able to induce autophagic flux, proteasomal activity and reduce the polyubiquitinated proteins by heat shock. PMID: 27975203
This study also suggests a malin function independent of laforin, possibly in lysosomal biogenesis and/or lysosomal glycogen disposal. PMID: 24914213
loss of laforin results in activation of serum/glucocorticoid-induced kinase 1 in cellular and animals models PMID: 24131995
expression of Epm2a blocks formation of Lafora bodies and restores the impairment in macroautophagy, preventing the development of Lafora bodies in Epm2a-deficient mice. PMID: 24430976
in laforin-deficient mice, stress drastically accelerates Lafora bodies accumulation and Lafora disease. PMID: 23546741
Results indicate that laforin has no effect on whole-body glucose metabolism and insulin sensitivity. PMID: 22186021
malin functions to regulate laforin and that malin deficiency at least in part causes LB and LD through increased laforin binding to glycogen. PMID: 22669944
Results show that a functional laforin-malin complex plays a critical role in disrupting Lafora bodies and relieving endoplasmic reticulum stres. PMID: 22578008
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. PMID: 22542948
Motor coordination, activity impairment, and memory deficits progressively increase with age in Epm2a deficient mice. PMID: 22487859
These results define laforin as a new regulator of insulin sensitivity. PMID: 21493628
Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice PMID: 12019206
Inactivation of Epm2a resulted in increased Wnt signaling and tumorigenesis PMID: 16959610
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
This study provides a molecular link between an observed biochemical property of laforin and the phenotype of a mouse model of Lafora disease. PMID: 18040046
laforin is a selective phosphatase for GSK-3beta and regulates cell cycle progression by GSK-3beta-dependent mechanisms and represses cyclin D1 expression PMID: 18824542
laforin functions to suppress excessive glycogen phosphorylation and is an essential component of the metabolism of normally structured glycogen, as shown in a mouse model PMID: 18852261
laforin and malin play a role protecting cells from ER-stress, likely contributing to the elimination of unfolded proteins PMID: 19529779
Study suggests that laforin is one of the critical regulators of Tau protein, that the NFTs could underlie some of the symptoms seen in Lafora disease. PMID: 19542233

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Subcellular Location

Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane.

Protein Families

Protein-tyrosine phosphatase family

Tissue Specificity

Detected in skeletal muscle and in brain (at protein level). Widely expressed. Higher levels of expression are found in heart, brain, liver, skeletal muscle and kidney.

Database Links

KEGG: mmu:13853

STRING: 10090.ENSMUSP00000066050

UniGene: Mm.89946

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Code	CSB-MP893415MO
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Recombinant Mouse Laforin (Epm2a)

Product Details

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Target Background

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