Analytical Data
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Gene name
construct
- Application
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Alternative Names
/
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Species
synthetic construct
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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
ABA03150.1
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Expression Region
1-353aa
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Molecular Weight
44.7 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 construct recombinant proteins has gained significant attention in the fields of biotechnology and molecular biology due to their pivotal role in understanding biological processes and developing therapeutic applications. Recombinant proteins are produced by inserting a gene of interest into a host organism, commonly bacteria, yeast, or mammalian cells, which then express the protein. This approach enables scientists to produce large quantities of proteins that can be used for various purposes, such as studying protein functions, developing vaccines, and generating monoclonal antibodies. Advances in genetic engineering techniques, including CRISPR and plasmid design, have facilitated the creation of tailored protein constructs that can enhance stability, solubility, and activity. Furthermore, the ability to participate in post-translational modifications in mammalian systems allows for more accurate mimicking of natural proteins. As a result, research on construct recombinant proteins is crucial in drug discovery, disease modeling, and the development of biopharmaceuticals, making it a critical area of exploration in modern science and medicine. The demand for effective therapies, especially in the context of emerging infectious diseases and genetic disorders, has accelerated the investigation of recombinant proteins, highlighting their importance as tools for innovation and therapeutic intervention.
