Analytical Data
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Gene name
like
- Application
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Alternative Names
Zinc finger CCCH domain-containing protein ZFN-like
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Species
Pisum sativum
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9SWF9
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Expression Region
1-417aa
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Molecular Weight
53 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 like reconstituted proteins has emerged as a pivotal area in molecular biology and biochemistry, driven by the need to understand protein structure and function at a detailed level. Proteins are essential biomolecules, playing critical roles in virtually every biological process. However, their inherent complexity and the challenges associated with isolating them in their native forms have prompted researchers to explore reconstitution methods. By utilizing techniques such as recombinant DNA technology, researchers can produce proteins in controlled environments, allowing for the examination of their properties, interactions, and folding behaviors. This approach not only aids in elucidating the mechanisms of protein function but also facilitates the design of therapeutic proteins and the development of novel biotechnological applications. Furthermore, the study of like reconstituted proteins provides insights into their evolutionary adaptations and potential roles in disease states. As advancements in structural biology and bioinformatics continue to evolve, the ability to reconstitute and study proteins in vitro holds promise for significant breakthroughs in drug discovery, synthetic biology, and understanding complex biological systems.
