Analytical Data
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Gene name
Z
- Application
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Alternative Names
Zinc-binding protein
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Species
Lassa virus
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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
O73557
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Expression Region
2-99aa
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Molecular Weight
14.6 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
The study of Z-recombinant proteins has gained significant attention in recent years due to their potential applications in biotechnology and medicine. Z-recombinant proteins, which are generated through genetic engineering techniques, allow for the production of proteins with modified properties for various purposes, including therapeutic interventions, vaccine development, and biocatalysis. The ability to manipulate protein structures enables researchers to enhance stability, increase efficacy, and reduce immunogenicity, making them highly suitable for use in treatment for diseases such as cancer and autoimmune disorders. The advancements in recombinant DNA technology, including CRISPR and advanced expression systems, have further accelerated the development of Z-recombinant proteins. Moreover, the ongoing demand for novel therapeutic agents has fueled research into optimizing production methods and improving purification processes. As a result, there is a growing body of literature exploring the biochemical, structural, and functional aspects of Z-recombinant proteins. This research not only aims to improve existing proteins but also to design entirely new proteins with tailor-made functions that meet specific medical needs. Overall, the exploration of Z-recombinant proteins represents a promising frontier in the field of molecular biology and has the potential to significantly impact healthcare outcomes in the future.
