Analytical Data
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Gene name
Mb
- Application
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Alternative Names
Mb；Myoglobin
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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
P02144
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Expression Region
1-154aa
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AA Sequence
MGLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGATVLTALGGILKKKGHHEAEIKPLAQSHATKHKIPVKYLEFISECIIQVLQSKHPGDFGADAQGAMNKALELFRKDMASNYKELGFQG
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Molecular Weight
17.1 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
Related Products
Protein Description
The research on Mb (myoglobin) recombinant proteins has gained significant attention due to their crucial role in various biochemical and biophysical processes, particularly in oxygen transport and storage within muscle tissues. Myoglobin, a heme-containing globin, is found primarily in vertebrate muscle cells and is essential for facilitating the diffusion of oxygen from the bloodstream to the mitochondria, where it is utilized for cellular respiration. With advancements in molecular biology techniques, recombinant DNA technology has enabled scientists to produce Mb in various host systems, such as bacteria, yeast, and mammalian cells. This has facilitated the study of Mb's structure-function relationships and its potential applications in biotechnology and medicine. Investigating the properties of recombinant Mb proteins, including their stability, folding, and interactions with ligands, can provide insights into muscle physiology and may lead to novel therapeutic strategies for conditions related to oxygen deficiency, such as ischemia and muscular dystrophies. Furthermore, the ability to engineer Mb with enhanced characteristics, such as increased oxygen affinity or stability under harsh conditions, opens up possibilities for its use in biosensors, oxygen scavengers, and biocatalysts. Thus, the study of Mb recombinant proteins not only enriches our understanding of fundamental biological processes but also paves the way for innovative applications in various fields, including medical diagnostics, environmental monitoring, and industrial biotechnology.
