Analytical Data
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Gene name
ZNF511
- Application
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Alternative Names
ZNF511; Zinc finger Protein 511
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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
Q8NB15
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Expression Region
1-252 aa
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AA Sequence
PLPVERDPAAGAAPFRFVARPVRFPREHQFFEDGDVQRHLYLQDVIMQVADVPEKPRVPAFACQVAGCCQVFDALDDYEHHYHTLHGNVCSFCKRAFPSGHLLDAHILEWHDSLFQILSERQDMYQCLVEGCTEKFKTSRDRKDHMVRMHLYPADFRFDKPKKSRSPASAEAPGDSGERSEGEAMEICSEPVAASPAPAGERRIYRHRIPSTICFGQGAARGFKSNKKKTKQC
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Molecular Weight
51.37 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
ZNF511 (Zinc Finger Protein 511) is a member of the zinc finger protein family, which is characterized by their ability to bind DNA and regulate gene expression. Research into ZNF511 has gained attention due to its emerging role in various biological processes, including cell differentiation, proliferation, and apoptosis. It is hypothesized that ZNF511 may play a critical part in cellular responses to stress and may also be involved in cancer progression and development. The study of recombinant ZNF511 protein allows scientists to explore its structural features and functional mechanisms in vitro. By producing ZNF511 in a controlled laboratory setting, researchers can investigate its interactions with other proteins, DNA binding capabilities, and its potential regulatory effects on gene expression. Moreover, understanding the precise role of ZNF511 could provide insights into its involvement in diseases, particularly in cancer, where dysregulation of transcription factors is common. As the need for targeted therapies increases, elucidating the function of ZNF511 may open new avenues for therapeutic interventions, making its study critical in both basic research and clinical applications.











