Analytical Data
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Gene name
MBP
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简介
MBP proteins, especially the classical isoforms 4-13, dominate myelin membranes in the central nervous system and are critical for myelination and stability. In contrast, the non-canonical isoform 1-3/Golli-MBP may be involved in early brain development and contribute to transcriptional complexes that influence multiple cellular processes. MBP Protein, Mouse (P.pastoris, His) is the recombinant mouse-derived MBP protein, expressed by P. pastoris , with N-6*His labeled tag.
- Application
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Alternative Names
MBP; Hmbpr; MGC99675; mld; Myelin A1 ; myelin basic; shi
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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
P04370
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Expression Region
M1-R250
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Protein Length
Full Length
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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
MBP (Maltose Binding Protein) is a widely used fusion tag in protein expression and purification, known for its ability to enhance solubility and facilitate the isolation of recombinant proteins. It originates from the Escherichia coli maltose operon and possesses a high affinity for maltose, making it an effective tool for chromatography applications. The research on MBP fusion proteins has gained momentum due to their versatility across various fields, including structural biology, enzymology, and therapeutic protein development. Scientists have leveraged MBP to improve the yields of otherwise challenging-to-express proteins, often resulting in properly folded and functional variants. Additionally, the use of MBP allows for the simplification of downstream purification processes, as these fusion proteins can be easily separated from host cell contaminants. Advances in MBP technology, including site-directed mutagenesis and novel purification methods, continue to enhance its utility. Recent studies have also explored the effects of MBP on protein stability and activity, providing insights into optimizing fusion tag systems for diverse applications. As research progresses, the understanding of MBP's role in protein engineering will further bolster its application in biotechnology and pharmaceutical industries, enabling the development of more effective diagnostic tools and therapeutic agents.
