Analytical Data
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Gene name
MYPN
- Application
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Alternative Names
MYOP; Sarcomeric Protein Myopalladin,145 kDa
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86TC9
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Expression Region
Pro945~Leu1320
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Molecular Weight
46kDa
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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
Related Products
Protein Description
MYPN (Myopalladin) is a crucial protein that plays an essential role in muscle structure and function, particularly in cardiac and skeletal muscle tissues. Research into MYPN and its recombinant forms has gained significant attention due to its involvement in various myopathies and cardiomyopathies. MYPN is part of the titin-associated protein family and is believed to contribute to the assembly and maintenance of the sarcomere, the fundamental unit of muscle contraction. Abnormalities in MYPN expression or function have been associated with genetic disorders that lead to muscle degeneration and heart failure. The development of recombinant MYPN proteins facilitates the study of its biochemical properties, interactions with other sarcomeric proteins, and its role in muscle pathology. Additionally, producing MYPN in a recombinant form enables researchers to explore its therapeutic potential in restoring muscle function or in drug design aimed at modulating its activity. Recent advancements in protein engineering and expression systems have improved the yield and functionality of recombinant MYPN, paving the way for detailed mechanistic studies and potential therapeutic applications in treating related muscular disorders. As research continues to unravel the complexities of MYPN's function and its implications in myopathies, it holds promise for advancing our understanding of muscle biology and developing targeted interventions for muscle-related diseases.
