Analytical Data
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Gene name
hykk
- Application
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Alternative Names
agphd1
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Species
Zebrafish
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A8WFT6
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Expression Region
1-355aa
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Molecular Weight
60.5 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
Hykk recombinant protein is a novel protein that has garnered significant interest in the field of biotechnology and biopharmaceuticals. Derived from the Hykk (Hypothetical protein K), this protein has been identified as a key player in various biological processes, including cellular signaling and immune responses. Research has shown that Hykk exhibits unique structural properties, making it a promising candidate for therapeutic applications. The ability to produce Hykk as a recombinant protein allows for large-scale production and detailed functional studies, enabling researchers to explore its potential as a drug candidate or vaccine component. Furthermore, the recombinant production system ensures a controlled environment for the protein's expression, which is crucial for maintaining its biological activity and stability. Studies involving Hykk recombinant protein have opened new avenues for understanding its role in disease mechanisms, particularly in immunological disorders and cancer. As research progresses, there is growing hope that Hykk could lead to innovative treatment strategies that harness its biological functions, emphasizing the importance of continued exploration in this exciting area of study.
