Analytical Data
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Gene name
RPB5
- Application
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Alternative Names
RPB5；DNA-directed RNA polymerases I. II. and III subunit RPABC1
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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
P19388
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Expression Region
1-210aa
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AA Sequence
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKVY CQRMQEENIT RALIVVQQGM TPSAKQSLVD MAPKYILEQF LQQELLINIT EHELVPEHVV MTKEEVTELL ARYKLRENQL PRIQAGDPVA RYFGIKRGQV VKIIRPSETA GRYITYRLVQ
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Molecular Weight
24.5 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
RPB5, a crucial subunit of RNA polymerase II, plays a significant role in the transcription of protein-coding genes by facilitating the assembly and stability of the polymerase complex. Research on RPB5 has been driven by its essential function in gene expression regulation and its involvement in various cellular processes. Abnormalities in RPB5 expression or function can lead to severe consequences, including developmental disorders and cancer. In recent years, studies have focused on the structural characteristics of RPB5, revealing its highly conserved nature across different species, suggesting its fundamental role in transcription mechanisms. Moreover, RPB5's interactions with other components of the transcription machinery highlight its importance in maintaining the fidelity of transcription and regulating gene expression in response to various environmental cues. By characterizing the properties of RPB5, researchers aim to uncover the intricate network of interactions that govern gene regulation, paving the way for potential therapeutic strategies targeting transcriptional dysregulation in disease contexts. Overall, the comprehensive understanding of RPB5 not only enhances our knowledge of fundamental biological processes but also opens up avenues for clinical applications in treating transcription-related pathologies.
