Analytical Data
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Gene name
ZNF566
- Application
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Alternative Names
ZNF566; Zinc finger Protein 566
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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
Q969W8
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Expression Region
1-418 aa
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AA Sequence
MAQESVMFSDVSVDFSQEEWECLNDDQRDLYRDVMLENYSNLVSMGHSISKPNVISYLEQGKEPWLADRELTRGQWPVLESRCETKKLFLKKEIYEIESTQWEIMEKLTRRDFQCSSFRDDWECNRQFKKELGSQGGHFNQLVFTHEDLPTLSHHPSFTLQQIINSKKKFCASKEYRKTFRHGSQFATHEIIHTIEKPYECKECGKSFRHPSRLTHHQKIHTGKKPFECKECGKTFICGSDLTRHHRIHTGEKPYECKECGKAFSSGSNFTRHQRIHTGEKPYECKECGKAFSSGSNFTQHQRIHTGEKPYECKECGNAFSQSSQLIKHQRIHTGEKPYECKECEKAFRSGSDLTRHQRIHTGEKPYECKICGKAYSQSSQLISHHRIHTSEKPYEYRECGKNFNYDPQLIQHQNLYW
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Molecular Weight
75.6 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
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Protein Description
ZNF566 is a member of the zinc finger protein family, which plays crucial roles in various biological processes, including gene regulation, cell differentiation, and development. Emerging research has highlighted its potential involvement in specific diseases, particularly in relation to cancer and neurological disorders. The ability of ZNF566 to bind DNA and modulate the transcription of target genes makes it a significant candidate for further investigation in the context of cellular function and disease pathology. The study of ZNF566 recombinant protein has garnered attention as it can provide insights into the protein's structure, function, and interaction with other molecular partners. Understanding the mechanistic pathways in which ZNF566 operates can unveil new therapeutic targets and strategies, particularly in cancer treatment where aberrant gene expression is a hallmark. Given the intricate interplay between zinc finger proteins and their regulatory roles, the characterization of ZNF566 through recombinant expression systems serves as a pivotal step toward elucidating its functional implications in health and disease. This research could pave the way for the development of novel diagnostic and therapeutic approaches, highlighting the importance of ZNF566 in the field of molecular biology and medicine.
