Analytical Data
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Gene name
MIT
- Application
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Alternative Names
Short name: MIT 1 Alternative name(s): Black mamba intestinal toxin 1 Black mamba venom protein A
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Species
Dendroaspis polylepis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P25687
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Expression Region
1-81aa
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Molecular Weight
24.6 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 recombinant proteins at the Massachusetts Institute of Technology (MIT) is grounded in the need to understand protein structure and function in biological systems. With advancements in molecular biology, MIT has focused on the production of recombinant proteins using various expression systems, such as bacteria, yeast, and mammalian cells. These proteins can be engineered to possess specific properties, enabling researchers to investigate their roles in cellular processes, develop targeted therapeutics, and enhance biotechnological applications. The use of recombinant DNA technology allows scientists to manipulate genes to produce proteins that may be difficult to extract from natural sources. This area of research is critical for the development of vaccines, enzymes for industrial applications, and protein-based drugs. Moreover, MIT's interdisciplinary approach integrates principles from bioengineering, computer science, and biophysics, enhancing the understanding of protein interactions and stability. Consequently, the research at MIT aims not only to advance fundamental knowledge in biochemistry but also to address real-world challenges such as disease treatment and sustainable production methods. Through collaboration and innovation, MIT continues to lead in the exploration of recombinant proteins, contributing to both scientific progress and technological breakthroughs.
