Analytical Data
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Gene name
prn
- Application
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Alternative Names
prn；MBN；Myeloblastin
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14283
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Expression Region
41-142aa
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AA Sequence
IVKTGERQHGIHIQGSDPGGVRTASGTTIKVSGRQAQGILLENPAAELQFRNGSVTSSGQLSDDGIRRFLGTVTVKAGKLVADHATLANVGDTWDDDGIALY
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Molecular Weight
17.6 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
PRN recombinant proteins are increasingly significant in the fields of biotechnology and medicine due to their diverse applications, including therapeutic uses, vaccine development, and diagnostic tools. PRN, or protein-recognition-neighbor, refers to a class of proteins that play critical roles in immune response and cellular mechanisms. The production of PRN recombinant proteins involves the use of genetic engineering techniques to insert the gene encoding the desired protein into host cells, such as bacteria or yeast, which then express the protein in large quantities. This approach offers several advantages, including the ability to produce complex proteins that might be difficult to obtain from natural sources, ensuring consistency and purity in production. Recent advancements in synthetic biology and proteomics have further enhanced the efficiency of PRN protein production and characterization. Researchers are exploring the immunogenic properties of these proteins to design novel vaccines, particularly against infectious diseases and cancers. Additionally, the study of PRN recombinant proteins contributes to our understanding of protein-protein interactions and their implications in various biological processes, paving the way for new therapeutic strategies. Overall, the ongoing research into PRN recombinant proteins holds immense potential for improving healthcare outcomes and developing innovative solutions to pressing medical challenges.
