Analytical Data
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Gene name
RNF208
- Application
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Alternative Names
1110061N23Rik; RGD1565957; RING finger protein 208; RN208_HUMAN; Rnf208; RP23-132N23.11-001
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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
Q9H0X6
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Expression Region
1-261 aa
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AA Sequence
MPSDPGPEAG SGWPGLLMSC LKGPHVILKM EAMKIVHPEK FPELPAAPCF PPAPRPTPTL APKRAWPSDT EIIVNQACGG DMPALEGAPH TPPLPRRPRK GSSELGFPRV APEDEVIVNQ YVIRPGPSAS AASSAAAGEP LECPTCGHSY NVTQRRPRVL SCLHSVCEQC LQILYESCPK YKFISCPTCR RETVLFTDYG LAALAVNTSI LSRLPPEALT APSGGQWGAE PEGSCYQTFR QYCGAACTCH VRNPLSACSI M
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Molecular Weight
27.9 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
RNF208 is an E3 ubiquitin ligase that plays a crucial role in the regulation of various cellular processes, including protein degradation, DNA repair, and cell cycle progression. This protein is known to mediate the polyubiquitination of target substrates, influencing their stability and function. Research has shown that RNF208 is involved in cancer biology, particularly in the modulation of tumor growth and metastasis, making it a potential biomarker for certain cancers. Understanding the mechanisms by which RNF208 exerts its effects could provide insights into tumorigenesis and may lead to the development of novel therapeutic strategies. Additionally, RNF208 is thought to be implicated in several neurodegenerative diseases, underscoring its importance beyond cancer research. However, the exact molecular pathways and interactions involving RNF208 remain to be fully elucidated. Therefore, the production of recombinant RNF208 protein is essential for conducting detailed biochemical assays and structural analyses, which can further the understanding of its functions and regulatory mechanisms. This research not only highlights RNF208’s potential as a therapeutic target but also contributes to the broader field of ubiquitin-mediated protein regulation in health and disease.
