Analytical Data
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Gene name
WIZ
- Application
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Alternative Names
WIZ;ZNF803;Protein Wiz
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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
O95785
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Expression Region
1228-1419aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSEFRTRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVPRELSLTPITGAKPSATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAH
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Molecular Weight
28.1 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
WIZ (Wiz, the putative zinc-finger protein) is a protein that has garnered attention in recent years due to its potential roles in cellular processes such as differentiation, proliferation, and apoptosis. Research indicates that WIZ may function as a transcriptional regulator, influencing gene expression through its interaction with various chromatin-modifying complexes. The restructuring of WIZ protein has become a focal point in understanding its functional mechanisms, especially concerning its involvement in various biological pathways and diseases, including cancer. Given the rising incidence of malignancies linked to aberrant cellular signaling and gene regulation, understanding the intricate role of WIZ can pave the way for novel therapeutic strategies. Investigations into the structural and functional aspects of WIZ are crucial, as they may reveal targets for pharmacological intervention. Moreover, the study of WIZ-recombinant proteins in cellular models can provide insights into how alterations in WIZ function contribute to disease pathogenesis, thereby highlighting its potential as a biomarker for cancer prognosis. Overall, dissecting the molecular workings of WIZ not only enhances our knowledge of fundamental biological processes but also offers promising avenues for developing targeted treatments in oncology and other related fields.











