Analytical Data
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Gene name
ZNFN1A5
- Application
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Alternative Names
Zinc finger protein Pegasus. Ikaros family zinc finger protein 5
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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
Q9H5V7
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Expression Region
2-100 aa
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AA Sequence
GEKKPEPLDFVKDFQEYLTQQTHHVNMISGSVSGDKEAEALQGAGTDGDQNGLDHPSVEVSLDENSGMLVDGFERTFDGKLKCRYCNYASKGTARLIEH
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Molecular Weight
36.63 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
ZNFN1A5, also known as Zinc Finger Protein 1A5, is a member of the zinc finger protein family, which are characterized by their ability to bind DNA and RNA, playing crucial roles in transcriptional regulation, signal transduction, and developmental processes. Research on ZNFN1A5 has gained momentum due to its potential implications in gene expression regulation and cellular differentiation, particularly in the context of various diseases, including cancers and genetic disorders. Understanding the structure and function of ZNFN1A5 through recombinant protein studies can provide insights into its biological mechanisms and interactions with other molecular partners. By producing ZNFN1A5 as a recombinant protein, researchers can investigate its binding affinities, post-translational modifications, and functional roles in cell signaling pathways. Such studies are essential for deciphering the complexities of gene regulatory networks within cells and may lead to the development of therapeutic strategies targeting abnormal protein functions associated with diseases. As the demand for effective treatments rises, elucidating the molecular underpinnings of ZNFN1A5 could pave the way for innovative approaches in precision medicine, making it a significant focus of contemporary biomedical research.
