Analytical Data
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Gene name
MYO
- Application
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Alternative Names
MYO；KIAA0865；MYO16B；NYAP3；Unconventional myosin-XVI
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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
Q92551
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Expression Region
1-441aa
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AA Sequence
MCVCQTMEVGQYGKNASRAGDRGVLLEPFIHQVGGHSSMMRYDDHTVCKPLISREQRFYESLPPEMKEFTPEYKGVVSVCFEGDSDGYINLVAYPYVESETVEQDDTTEREQPRRKHSRRSLHRSGSGSDHKEEKASLSLETSESSQEAKSPKVELHSHSEVPFQMLDGNSGLSSEKISHNPWSLRCHKQQLSRMRSESKDRKLYKFLLLENVVHHFKYPCVLDLKMGTRQHGDDASAEKAARQMRKCEQSTSATLGVRVCGMQVYQLDTGHYLCRNKYYGRGLSIEGFRNALYQYLHNGLDLRRDLFEPILSKLRGLKAVLERQASYRFYSSSLLVIYDGKECRAESCLDRRSEMRLKHLDMVLPEVASSCGPSTSPSNTSPEAGPSSQPKVDVRMIDFAHSTFKGFRDDPTVHDGPDRGYVFGLENLISIMEQMRDENQ
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Molecular Weight
66.2kDa
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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
MYO recombinant proteins, derived from the MYO gene family, have garnered significant attention in recent years due to their critical roles in various biological processes, including muscle contraction, cellular signaling, and cytoskeletal organization. These proteins are characterized by their myosin-like structure, which enables them to interact effectively with actin filaments, playing a pivotal role in muscle physiology and other cellular movements. Research into MYO recombinant proteins has expanded as scientists seek to understand their unique functions and regulatory mechanisms in both normal physiology and disease states, such as cardiomyopathies and skeletal muscle disorders. The production of MYO recombinant proteins through advanced biotechnological methods allows for the investigation of their structural and functional properties in a controlled environment, facilitating insights into their potential therapeutic applications. Additionally, by employing techniques such as gene editing and protein engineering, researchers aim to create modified versions of these proteins that can serve as biopharmaceuticals or as tools for elucidating cellular mechanisms. The study of MYO recombinant proteins holds promise not only for elucidating fundamental biological processes but also for translating findings into innovative treatments for muscle-related diseases and other pathologies, thereby bridging fundamental research with applied biomedical sciences.
