Analytical Data
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Gene name
ZNF100
- Application
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Alternative Names
ZNF100Zinc finger Protein 100
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IYN0
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Expression Region
1-109 aa
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AA Sequence
MDDPRYGMCPLKGASGCPGAERSLLVQSYFEKGPLTFRDVAIEFSLEEWQ CLDSAQQGLYRKVMLENYRNLVFLAGIALTKPDLITCLEQGKEPWNIKRH EMVAKPPVI
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Molecular Weight
12 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
ZNF100, also known as zinc finger protein 100, is a member of the zinc finger protein family, which plays a crucial role in various biological processes, including transcription regulation, DNA repair, and cell differentiation. Its unique structure, characterized by multiple zinc finger motifs, allows it to bind to specific DNA sequences, thereby influencing gene expression and cellular function. Research into ZNF100 has gained momentum due to its potential implications in cancer biology and developmental disorders. Studies have indicated that abnormal expression or mutations in ZNF100 could be linked to tumorigenesis, making it a candidate for further investigation as a biomarker or therapeutic target. Furthermore, understanding the molecular mechanisms underlying ZNF100's functions may provide insights into broader regulatory networks and cellular pathways. Recent advances in protein engineering and recombinant DNA technology have enabled the development of ZNF100 recombinant proteins, facilitating detailed studies of its interaction with other biomolecules and its role in cellular processes. This research holds promise not only for elucidating the fundamental biology of zinc finger proteins but also for potential applications in gene therapy and personalized medicine, paving the way for innovative strategies to combat diseases associated with ZNF100 dysregulation.
