Cat: PA2000-9527

Recombinant Human MTMR10 Protein,His

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Analytical Data

  • Gene name

    MTMR10

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MTMR10; Myotubularin-related protein 10; Inactive phosphatidylinositol 3-phosphatase 10

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9NXD2

  • Expression Region

    1-777 aa

  • AA Sequence

    MFSLKPPKPT FRSYLLPPPQ TDDKINSEPK IKKLEPVLLP GEIVVNEVNF VRKCIATDTS QYDLWGKLIC SNFKISFITD DPMPLQKFHY RNLLLGEHDV PLTCIEQIVT VNDHKRKQKV LGPNQKLKFN PTELIIYCKD FRIVRFRFDE SGPESAKKVC LAIAHYSQPT DLQLLFAFEY VGKKYHNSAN KINGIPSGDG GGGGGGGNGA GGGSSQKTPL FETYSDWDRE IKRTGASGWR VCSINEGYMI STCLPEYIVV PSSLADQDLK IFSHSFVGRR MPLWCWSHSN GSALVRMALI KDVLQQRKID QRICNAITKS HPQRSDVYKS DLDKTLPNIQ EVQAAFVKLK QLCVNEPFEE TEEKWLSSLE NTRWLEYVRA FLKHSAELVY MLESKHLSVV LQEEEGRDLS CCVASLVQVM LDPYFRTITG FQSLIQKEWV MAGYQFLDRC NHLKRSEKES PLFLLFLDAT WQLLEQYPAA FEFSETYLAV LYDSTRISLF GTFLFNSPHQ RVKQSTEFAI SKNIQLGDEK GLKFPSVWDW SLQFTAKDRT LFHNPFYIGK STPCIQNGSV KSFKRTKKSY SSTLRGMPSA LKNGIISDQE LLPRRNSLIL KPKPDPAQQT DSQNSDTEQY FREWFSKPAN LHGVILPRVS GTHIKLWKLC YFRWVPEAQI SLGGSITAFH KLSLLADEVD VLSRMLRQQR SGPLEACYGE LGQSRMYFNA SGPHHTDTSG TPEFLSSSFP FSPVGNLCRR SILGTPLSKF LSGAKIWLST ETLANED

  • Molecular Weight

    88.2 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

The MTMR10 protein, part of the myotubularin family, has gained significant attention in recent years due to its potential implications in various cellular processes and diseases. Myotubularins are phosphoinositide phosphatases that play crucial roles in lipid metabolism and intracellular signaling by dephosphorylating phosphoinositides, which are key regulators of cellular functions, including vesicle trafficking and membrane dynamics. MTMR10 has been particularly studied for its involvement in muscle development and function, as mutations in myotubularin family members are associated with muscle disorders such as centronuclear myopathy and Charcot-Marie-Tooth disease. Recent research indicates that MTMR10 may also have roles beyond muscle tissue, including impacts on neuronal health and inflammatory responses. Advancements in recombinant protein technology have enabled the production and purification of MTMR10, facilitating investigations into its functional properties and interactions with other cellular components. Understanding the structure-function relationship of MTMR10 at a molecular level is crucial for deciphering its roles in health and disease, paving the way for potential therapeutic strategies targeting myotubularin pathways. As such, the study of MTMR10 is not only important for elucidating the underlying mechanisms of muscle-related pathologies but also holds promise for broader biomedical applications involving phosphoinositide signaling.

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