Analytical Data
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Gene name
ZRANB2
- Application
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Alternative Names
ZRANB2;ZIS;ZNF265;Zinc finger Ran-binding domain-containing Protein 2
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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
O95218
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Expression Region
1-320aa
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AA Sequence
MSTKNFRVSDGDWICPDKKCGNVNFARRTSCNRCGREKTTEAKMMKAGGTEIGKTLAEKSRGLFSANDWQCKTCSNVNWARRSECNMCNTPKYAKLEERTGYGGGFNERENVEYIEREESDGEYDEFGRKKKKYRGKAVGPASILKEVEDKESEGEEEDEDEDLSKYKLDEDEDEDDADLSKYNLDASEEEDSNKKKSNRRSRSKSRSSHSRSSSRSSSPSSSRSRSRSRSRSSSSSQSRSRSSSRERSRSRGSKSRSSSRSHRGSSSPRKRSYSSSSSSPERNRKRSRSRSSSSGDRKKRRTRSRSPESQVIGENTKQP
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Molecular Weight
52.3 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
ZRANB2, or Zinc Finger RNA Binding Protein 2, is a crucial member of the zinc finger protein family, known for its role in RNA processing and regulation. Research has indicated that ZRANB2 participates in various cellular processes, including RNA splicing, transcription regulation, and mRNA stability, which are vital for maintaining cellular homeostasis. Abnormal expression or mutations in ZRANB2 have been associated with several diseases, including certain types of cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. Previous studies have suggested that ZRANB2 interacts with other proteins involved in RNA metabolism, suggesting a complex regulatory network that warrants further investigation. The recombinant protein of ZRANB2 can be used to elucidate its functional mechanisms and interactions in vitro, providing insights into its role in normal biological processes and disease states. Understanding the structure-function relationship of ZRANB2 is essential for developing novel therapeutic strategies aimed at modulating its activity in pathological conditions. Recent advancements in protein engineering and purification techniques have enabled researchers to obtain sufficient quantities of functional recombinant ZRANB2, facilitating detailed biochemical and biophysical characterizations that can further unravel its significance in RNA biology. This research holds promise for uncovering new avenues in gene regulation and cellular function, paving the way for innovative approaches to disease treatment.











