Analytical Data
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Gene name
NFIX
- Application
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Alternative Names
NF1A; CTF; CCAAT-Binding Transcription Factor; TGGCA-binding protein
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Species
Rat
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
F2Z3R4
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Expression Region
His13~Thr298
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Molecular Weight
63kDa
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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
The NFIX (Nuclear Factor I X) protein plays a crucial role in various biological processes, including cell growth, differentiation, and developmental signaling pathways. It belongs to the Nuclear Factor I (NFI) family of transcription factors, which are vital for the regulation of genes involved in the development of the nervous system and other tissues. Research has shown that NFIX is implicated in multiple neurological disorders and conditions, highlighting its potential as a therapeutic target. The study of NFIX recombinant proteins has gained traction due to their ability to mimic the native protein’s functions in various assays, providing insights into its mechanisms of action. Through the use of molecular biology techniques, researchers have been able to produce NFIX recombinant proteins, enabling detailed investigations into their structure, stability, and interactions with DNA and other proteins. Understanding these interactions is essential for elucidating the protein's role in gene regulation and its impact on cellular processes. Additionally, the recombinant NFIX protein serves as a valuable tool for the development of potential therapeutic strategies aimed at correcting dysfunctions related to NFIX in human diseases. As interest in NFIX continues to grow, research surrounding its recombinant forms will likely facilitate advancements in targeted gene therapy and molecular medicine approaches, ultimately contributing to better diagnostic and therapeutic solutions for conditions linked to NFIX dysregulation.
