Analytical Data
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Gene name
ZNF483
- Application
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Alternative Names
ZNF483; KIAA1962; ZKSCAN16Zinc finger Protein 483; Zinc finger Protein with KRAB and SCAN domains 16
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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
Q8TF39
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Expression Region
1-244 aa
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AA Sequence
MQAVVPLNKMTAISPEPQTLASTEQNEVPRVVTSGEQEAILRGNAADAESFRQRFRWFCYSEVAGPRKALSQLWELCNQWLRPDIHTKEQILELLVFEQFLTILPGEIRIWVKSQHPESSEEVVTLIEDLTQMLEEKDPVSQDSTVSQEENSKEDKMVTVCPNTESCESITLKDVAVNFSRGEWKKLEPFQKELYKEVLLENLRNLEFLDFPVSKLELISQLKWVELPWLLEEVSKSSRLGSVI
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Molecular Weight
54.5 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
ZNF483, a member of the zinc finger protein family, is of particular interest in genomic research due to its potential roles in transcriptional regulation, cellular differentiation, and disease development. Initial studies have linked ZNF483 to various cellular processes, suggesting its involvement in gene expression modulation. Recent advances in molecular biology techniques have facilitated the production and characterization of recombinant ZNF483 protein, enabling researchers to explore its structure-function relationship in greater detail. The reconstitution of ZNF483 as a recombinant protein allows for the examination of its specific binding interactions with DNA and other regulatory proteins, shedding light on its role within complex genetic networks. Furthermore, there is growing evidence that ZNF483 may be implicated in cancer progression and other pathologies, warranting further investigation into its potential as a therapeutic target. By studying the functional properties of ZNF483 through recombination, scientists aim to uncover its contributions to molecular pathways critical for normal cellular function and disease states, paving the way for novel approaches in biomedical research and therapeutic innovation.
