Analytical Data
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Gene name
OP
- Application
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Alternative Names
Antifreeze protein lambda OP-3
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Species
Zoarces americanus
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Source
E. coli
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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
P19606
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Expression Region
23-91aa
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Molecular Weight
11.6 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
OP (Oligomeric Protein) recombinant proteins have garnered significant attention in recent years due to their potential applications in biotechnology and medicine. These proteins, which are produced through recombinant DNA technology, allow for the study and manipulation of complex biological functions, paving the way for advancements in various fields such as drug development, vaccine production, and therapeutic interventions. Research on OP recombinant proteins focuses on understanding their structure, function, and interactions within cellular environments. By harnessing the capabilities of genetic engineering, scientists can create specific protein variants that exhibit desired properties, such as increased stability, enhanced activity, or improved binding affinities. This has profound implications for drug design, particularly in the development of targeted therapies for diseases like cancer, where precise molecular interactions are crucial. Additionally, the ability to produce these proteins in large quantities provides a sustainable and efficient means of generating essential biological materials needed for research and treatment. Overall, the ongoing exploration of OP recombinant proteins stands at the intersection of molecular biology and therapeutic innovation, driving forward the potential for groundbreaking solutions to pressing health challenges.
