Analytical Data
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Gene name
MBP/MalE
- Application
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Alternative Names
PRG2; BMPG; Proteoglycan 2; Bone Marrow,Natural Killer Cell Activator; Eosinophil Granule Major Basic Protein; Proteoglycan 2,Bone Marrow; Pregnancy-associated major basic
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Species
Rat
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q63189
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Expression Region
Gly80~Lys219
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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
The study of MBP (Maltose-Binding Protein) and MalE (the periplasmic maltose-binding protein from Escherichia coli) recombinant proteins has gained significant attention due to their crucial roles in molecular biology and biotechnology. MBP, known for its ability to enhance the solubility and stability of fused proteins, is frequently utilized as a tag for protein purification and characterization. By forming stable complexes with maltose, MBP facilitates the efficient isolation of target proteins via affinity chromatography, often improving yields and functionality. MalE, on the other hand, is integral to the bacterial maltose transport system and serves as a model for studying protein folding and transport mechanisms in Gram-negative bacteria. Researchers have leveraged recombinant technology to produce MBP and MalE for various applications, including structural biology, vaccine development, and enzyme engineering. Understanding the functional and structural properties of these proteins enables advancements in therapeutic protein production, as well as the development of novel biocatalysts. The exploration of MBP and MalE also contributes to the broader understanding of protein interactions and cellular processes, highlighting their importance in both basic research and applied sciences. As such, the recombinant production of these proteins continues to be a significant focus in the field of protein engineering and will likely play a pivotal role in future biotechnological innovations.
