Analytical Data
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Gene name
mtb12
- Application
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Alternative Names
CFP-2 Low molecular weight protein antigen 2
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Species
Mycobacterium tuberculosis
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P9WIN6
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Expression Region
49-168aa
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Molecular Weight
14.1 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
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Protein Description
MTB12 is a recombinant protein derived from the Escherichia coli bacterium, which has garnered significant interest in the fields of molecular biology and biotechnology. The MTB12 protein is particularly notable for its role in the regulation of various metabolic processes within bacterial cells, making it a valuable tool for understanding cellular functions and interactions. Research into MTB12 is driven by the need to explore its potential applications in synthetic biology, where it could be employed to develop novel biosensors or metabolic pathways for bioproduction. Additionally, MTB12 serves as a useful model for studying protein folding and stability, providing insights into protein engineering and therapeutic development. The exploration of MTB12 encompasses various techniques such as gene cloning, protein expression, purification, and characterization. Through these studies, researchers aim to elucidate the structure-function relationships of MTB12, paving the way for innovative solutions in medicine and environmental science. The growing body of literature on MTB12 underlines its importance as a multifunctional protein, shedding light on its diverse biological roles and potential for practical applications.
