Analytical Data
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Gene name
MYOT
- Application
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Alternative Names
MYOT；TTID；Myotilin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UBF9
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Expression Region
1-498aa
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AA Sequence
MFNYERPKHF IQSQNPCGSR LQPPGPETSS FSSQTKQSSI IIQPRQCTEQ RFSASSTLSS HITMSSSAFP ASPKQHAGSN PGQRVTTTYN QSPASFLSSI LPSQPDYNSS KIPSAMDSNY QQSSAGQPIN AKPSQTANAK PIPRTPDHEI QGSKEALIQD LERKLKCKDT LLHNGNQRLT YEEKMARRLL GPQNAAAVFQ AQDDSGAQDS QQHNSEHARL QVPTSQVRSR STSRGDVNDQ DAIQEKFYPP RFIQVPENMS IDEGRFCRMD FKVSGLPAPD VSWYLNGRTV QSDDLHKMIV SEKGLHSLIF EVVRASDAGA YACVAKNRAG EATFTVQLDV LAKEHKRAPM FIYKPQSKKV LEGDSVKLEC QISAIPPPKL FWKRNNEMVQ FNTDRISLYQ DNTGRVTLLI KDVNKKDAGW YTVSAVNEAG VTTCNTRLDV TARPNQTLPA PKQLRVRPTF SKYLALNGKG LNVKQAFNPE GEFQRLAAQS GLYESEEL
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Molecular Weight
55.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
MYOT (myotilin) is a protein that plays a crucial role in muscle structure and function, and its research has gained significant attention in the context of muscular disorders, particularly in myopathies. Disruptions in MYOT have been linked to various genetic conditions, notably those affecting skeletal muscle integrity. The study of MYOT is fundamental for understanding the molecular mechanisms underlying muscle function and the pathogenesis of myopathies, including variants like nemaline myopathy and other congenital myopathies. Recent advances in molecular biology and genetic techniques have allowed researchers to explore the implications of MYOT mutations on muscle cell architecture and contractility. Investigations into MYOT often involve the generation of recombinant MYOT proteins to study their interactions with other muscle proteins and to elucidate the pathways affected by MYOT deficiencies. Such studies are vital for developing targeted therapies and improving diagnostic approaches for patients with MYOT-related disorders. As the research progresses, the hope is that a deeper understanding of MYOT's biological role will lead to novel therapeutic strategies for restoring muscle function in affected individuals, providing a significant benefit to both patients and the field of muscle biology.
