Analytical Data
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Gene name
ZAN
- Application
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Alternative Names
ZAN; ZAN_HUMAN; Zonadhesin
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y493
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Expression Region
1-113 aa
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AA Sequence
KEKPPDQKLVVRSSRDNYVLTQCDFEDDAKPLCDWSQVSADDEDWVRASGPSPTGSTGAPGGYPNGEGSYLHMESNSFHRGGVARLLSPDLWEQG
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Molecular Weight
36.19 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
ZAN (Zinc-binding Antiviral Protein) is an important component in the field of virology and molecular biology, primarily due to its role in the innate immune response. Its significance has escalated in the context of emerging viral infections and the urgent need for novel therapeutics and vaccines. ZAN's ability to bind zinc ions suggests a potential mechanism through which it exerts antiviral effects, as zinc is known to possess antiviral properties and can modulate various cellular processes. Research has indicated that ZAN is involved in inhibiting viral replication and modulating immune responses, making it a promising target for developing antiviral strategies. Furthermore, the ongoing studies aim to elucidate its structure-function relationships, enabling scientists to engineer recombinant ZAN proteins. These recombinant proteins can serve not only as potential therapeutics but also as valuable tools in vaccine development. The increasing understanding of ZAN's interactions with different viral proteins and its role in immunity is paving the way for innovative approaches to combat viral infections. As researchers continue to explore the applications of recombinant ZAN in therapeutic and preventive measures, its significance in translational research is becoming increasingly evident, highlighting the need for further studies that could ultimately lead to breakthroughs in antiviral drug development and vaccine efficacy.
