Analytical Data
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Gene name
ZNF396
- Application
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Alternative Names
ZNF396; ZSCAN14Zinc finger Protein 396; Zinc finger and SCAN domain-containing Protein 14
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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
Q96N95
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Expression Region
1-335 aa
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AA Sequence
MSAKLGKSSS LLTQTSEECN GILTEKMEEE EQTCDPDSSL HWSSSYSPET FRQQFRQFGY QDSPGPHEAL SRLWELCHLW LRPEVHTKEQ ILELLVLEQF LAILPKELQA WVQKHHPENG EETVTMLEDV ERELDGPKQI FFGRRKDMIA EKLAPSEITE ELPSSQLMPV KKQLQGASWE LQSLRPHDED IKTTNVKSAS RQKTSLGIEL HCNVSNILHM NGSQSSTYRG TYEQDGRFEK RQGNPSWKKQ QKCDECGKIF SQSSALILHQ RIHSGKKPYA CDECAKAFSR SAILIQHRRT HTGEKPYKCH DCGKAFSQSS NLFRHRKRHI RKKVP
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Molecular Weight
38.6 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
ZNF396, a member of the zinc finger protein family, plays a crucial role in various biological processes, including transcription regulation and DNA binding. Recent studies have highlighted its involvement in cellular functions such as proliferation, differentiation, and stress response. Given its potential implications in cancer biology and other diseases, there is an increasing interest in understanding the structure-function relationship of ZNF396. The recombinant expression of ZNF396 allows researchers to produce and purify the protein for functional assays, binding studies, and structural analysis. This enables the investigation of its interaction with DNA and other proteins, shedding light on its mechanistic role in gene regulation. The elucidation of ZNF396’s function is pivotal for exploring therapeutic avenues, particularly in cancer treatment and regenerative medicine. Furthermore, investigating its post-translational modifications could provide insights into the regulatory mechanisms governing its activity and stability. As research progresses, recombinant ZNF396 is expected to serve as a valuable tool for unveiling its biological significance and therapeutic potential.
