Analytical Data
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Gene name
CDO
- Application
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Alternative Names
Cysteine dioxygenase type I
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16878
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Expression Region
1-200aa
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Molecular Weight
50 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 study of chimeric disulfide-bonded oligomers (CDOs) has gained significant interest in protein engineering and therapeutic development. CDOs are proteins that have been modified to contain disulfide bonds between different protein domains, which can enhance their stability, solubility, and functionality. This strategic reorganization of protein structure allows for improved therapeutic properties, such as increased resistance to proteolysis and improved pharmacokinetics. Researchers are particularly drawn to the potential of CDOs in the design of biopharmaceuticals, including monoclonal antibodies and therapeutic enzymes, as the unique structural configurations can lead to novel mechanisms of action and targeted delivery. Advances in analytical techniques, such as mass spectrometry and X-ray crystallography, have facilitated deeper insights into the folding and behavior of CDOs, aiding in the optimization of their properties. Moreover, the ability to regulate the formation of disulfide bonds through various chemical and genetic methods enhances the versatility of CDOs in diverse applications. As the demand for innovative therapeutic options continues to rise, understanding the complex interactions and stability of CDOs is paramount in advancing drug design and improving patient outcomes.
