Analytical Data
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Gene name
p200
- Application
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Alternative Names
p200; MPN_567; MP275; Protein P200
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Species
Mycoplasma pneumoniae
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P75211
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Expression Region
857-985aa
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Molecular Weight
23.2 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 recombinant P200 proteins has garnered significant interest due to their potential applications in therapeutic and biotechnological fields. P200, a protein associated with various biological processes, including immune response and cell signaling, has been identified as a key player in several diseases, including cancer and autoimmune disorders. Researchers aim to understand its structure-function relationships to develop novel diagnostic tools and treatments. The ability to produce P200 in a recombinant form allows for detailed biochemical and biophysical characterization, enabling scientists to investigate its functional roles in cellular pathways. Furthermore, recombinant P200 can serve as a valuable resource for generating specific antibodies or inhibitors, aiding in elucidating the underlying mechanisms of pathologies. With advancements in molecular biology techniques, the optimization of expression systems and purification strategies for recombinant P200 has improved, facilitating its study in various models. Overall, the exploration of recombinant P200 proteins presents a promising frontier for enhancing our understanding of disease mechanisms and developing innovative therapeutic strategies.
