Analytical Data
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Gene name
ZNF212
- Application
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Alternative Names
Zinc finger protein C2H2-150
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UDV6
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Expression Region
1-495aa
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Molecular Weight
71.4 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
ZNF212 (Zinc Finger Protein 212) is a member of the zinc finger protein family, which is known for its role in DNA binding and transcription regulation. This protein is of significant interest due to its potential involvement in various biological processes, including cell differentiation, proliferation, and apoptosis. Recent studies have suggested that ZNF212 may play a role in cancer biology, particularly in the regulation of tumor suppressor genes and oncogenes. As researchers continue to uncover the molecular mechanisms underlying ZNF212 function, the production of recombinant ZNF212 protein has become crucial for functional assays, structural studies, and therapeutic development. By generating and characterizing this recombinant protein, scientists aim to elucidate its specific interactions and regulatory pathways, thereby enhancing our understanding of its contributions to cellular homeostasis and disease states. Additionally, the study of ZNF212 may pave the way for novel therapeutic strategies targeting its signaling pathways in cancer and other diseases. Overall, the investigation of ZNF212 and its recombinant form represents a promising area of research in molecular biology and medicine.











