Analytical Data
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Gene name
POLR2J
- Application
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Alternative Names
AATF;CHE1;DED;Protein AATF
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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
P52435
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Expression Region
1-117aa
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AA Sequence
MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG YKVPHPLEHK IIIRVQTTPD YSPQEAFTNA ITDLISELSL LEERFRVAIK DKQEGIE
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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
Polymerase II (POLR2J) is a crucial component of the RNA polymerase II complex, responsible for transcribing DNA into mRNA in eukaryotic cells. This complex is essential for gene expression regulation and is involved in various cellular processes, including cell differentiation, response to stress, and development. Dysregulation of RNA polymerase II activity has been implicated in numerous diseases, including cancer and neurodegenerative disorders, making the understanding of its subunits, like POLR2J, particularly important. Research on POLR2J has revealed its role in the modulation of transcriptional dynamics and its interaction with various transcription factors and regulatory proteins. The recombinant expression of POLR2J allows for detailed studies of its structural properties, functional mechanisms, and interaction networks. Furthermore, characterizing POLR2J through recombinant protein techniques can aid in the identification of potential therapeutic targets and enhance our understanding of transcription machinery in health and disease. Given the pivotal role of RNA polymerase II in gene regulation, the functional analysis of POLR2J offers promising insights into the molecular mechanisms governing gene expression, ultimately contributing to advancements in biomedical research and therapeutic development.
