Analytical Data
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Gene name
Myoglobin
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简介
Myoglobin Protein, a crucial member of the globin family, acts as a reserve oxygen supply, facilitating efficient oxygen transport within muscles.Myoglobin Protein, Mouse (P.pastoris, His) is the recombinant mouse-derived Myoglobin protein, expressed by P.pastoris , with C-Myc, N-6*His labeled tag.
- Application
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Alternative Names
Mb; Myoglobin
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Species
Mouse
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Source
P. pastoris
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04247
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Expression Region
G2-G154
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Protein Length
Full Length of Mature Protein
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Molecular Weight
21 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
Myoglobin (Mb) is a critical heme-containing protein found primarily in muscle tissues, playing a vital role in oxygen storage and transport. The study of recombinant myoglobin has garnered significant interest due to its implications in understanding muscle physiology, oxygen-binding mechanisms, and potential biomedical applications. Recombinant DNA technology allows for the expression of myoglobin in various host systems, such as bacteria, yeast, or mammalian cells, thus providing a powerful tool to produce large quantities of the protein for in-depth research. Investigating the structure-function relationship of myoglobin helps elucidate how mutations can affect its oxygen affinity and stability, which is essential for understanding certain myopathies and improving muscle performance. Additionally, recombinant myoglobin serves as a model for studying heme protein folding and refolding processes, offering insights that can be applied in protein engineering and drug design. The ability to modify myoglobin through site-directed mutagenesis further enhances its utility in biotechnological applications, including biosensors and bioartificial organs. The ongoing research into recombinant myoglobin thus not only contributes to fundamental scientific knowledge but also paves the way for innovative therapeutic strategies and advancements in tissue engineering. Overall, the exploration of recombinant myoglobin continues to be a vibrant area of research with broad implications across multiple fields, from basic biology to clinical applications.
