Analytical Data
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Gene name
RPRD1B
- Application
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Alternative Names
RPRD1B;C20orf77;CREPT;Regulation of nuclear pre-mRNA domain-containing Protein 1B
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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
Q9NQG5
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Expression Region
1-326aa
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AA Sequence
MSSFSESALE KKLSELSNSQ QSVQTLSLWL IHHRKHAGPI VSVWHRELRK AKSNRKLTFL YLANDVIQNS KRKGPEFTRE FESVLVDAFS HVAREADEGC KKPLERLLNI WQERSVYGGE FIQQLKLSME DSKSPPPKAT EEKKSLKRTF QQIQEEEDDD YPGSYSPQDP SAGPLLTEEL IKALQDLENA ASGDATVRQK IASLPQEVQD VSLLEKITDK EAAERLSKTV DEACLLLAEY NGRLAAELED RRQLARMLVE YTQNQKDVLS EKEKKLEEYK QKLARVTQVR KELKSHIQSL PDLSLLPNVT GGLAPLPSAG DLFSTD
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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
RPRD1B, or the RNA Polymerase II Readthrough and Recruitment Domain 1B, is a protein that plays a crucial role in the regulation of transcription and mRNA processing. It is known to be involved in the recruitment of various factors to the transcription machinery, influencing RNA polymerase II activity and promoting the elongation phase of transcription. Recent research highlights its significance in the context of various cellular processes, including gene expression regulation, response to DNA damage, and cell cycle progression. Dysregulation of RPRD1B has been implicated in several diseases, including cancer, where altered transcriptional control can lead to oncogenesis. Studies have demonstrated that RPRD1B interacts with specific transcription factors and co-regulators, contributing to the modulation of transcriptional outcomes. Understanding the structure and function of RPRD1B, as well as its interactions with other proteins, is crucial for elucidating its role in cellular function and disease. Current research efforts focus on characterizing the biochemical properties of the RPRD1B protein, exploring its potential as a therapeutic target, and investigating the mechanistic pathways through which it affects gene expression. The ongoing investigation into RPRD1B is paving the way for novel insights into transcriptional regulation and its implications in both normal physiology and disease states.
