Analytical Data
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Gene name
Rbck1
- Application
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Alternative Names
(Heme-oxidized IRP2 ubiquitin ligase 1 homolog)(HOIL-1)(Protein kinase C-binding protein beta-15)(RBCC protein interacting with PKC)(RING-type E3 ubiquitin transferase HOIL-1)(Ubiquitin-conjugating enzyme 7-interacting protein 3)
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Species
Rat
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q62921
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Expression Region
1-508aa
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Molecular Weight
65.1 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
Rbck1, or RING finger and CHY zinc finger domain-containing protein 1, is a member of the RING-type E3 ubiquitin ligase family, which plays a crucial role in the ubiquitin-proteasome system, a key cellular mechanism for regulating protein degradation and signaling. The enzyme's unique structure allows it to facilitate the transfer of ubiquitin moieties to target proteins, thereby influencing various cellular processes, including cell cycle progression, DNA repair, and immune responses. Recent studies have highlighted Rbck1's involvement in various pathophysiological conditions, such as cancer and neurodegenerative diseases, suggesting that dysregulation of Rbck1 may contribute to aggressive tumor phenotypes and neuronal loss. Researchers are increasingly focused on understanding the specific substrates of Rbck1 and its regulatory mechanisms to uncover its potential as a therapeutic target. The development of recombinant Rbck1 proteins allows for a deeper investigation into its functional roles and interactions within cellular pathways, fostering advancements in targeted therapies. Given the rising significance of ubiquitin ligases in drug development and disease management, studying Rbck1 could provide novel insights into innovative treatments for disease intervention. As a result, creating and characterizing Rbck1 recombinant proteins is a pivotal step toward unraveling its complex biology and therapeutic potential.
