Analytical Data
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Gene name
RNF32
- Application
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Alternative Names
RNF32; FKSG33; HSD15; RING finger protein 32
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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
Q9H0A6
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Expression Region
1-362 aa
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AA Sequence
MLKNKGHSSK KDNLAVNAVA LQDHILHDLQ LRNLSVADHS KTQVQKKENK SLKRDTKAII DTGLKKTTQC PKLEDSEKEY VLDPKPPPLT LAQKLGLIGP PPPPLSSDEW EKVKQRSLLQ GDSVQPCPIC KEEFELRPQV LLSCSHVFHK ACLQAFEKFT NKKTCPLCRK NQYQTRVIHD GARLFRIKCV TRIQAYWRGC VVRKWYRNLR KTVPPTDAKL RKKFFEKKFT EISHRILCSY NTNIEELFAE IDQCLAINRS VLQQLEEKCG HEITEEEWEK IQVQALRRET HECSICLAPL SAAGGQRVGA GRRSREMALL SCSHVFHHAC LLALEEFSVG DRPPFHACPL CRSCYQKKIL EC
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Molecular Weight
41.5 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
RNF32, a member of the RING finger protein family, serves as a vital E3 ubiquitin ligase that plays a significant role in diverse cellular processes, including protein degradation, cell cycle regulation, and stress responses. Recent studies have highlighted its involvement in various diseases, particularly cancer, where it is implicated in the regulation of tumor suppressor genes and oncogenes through ubiquitination pathways. The understanding of RNF32’s function has expanded with advancements in proteomic technologies, enabling researchers to identify its substrates and interacting partners. This has prompted interest in characterizing its structure and elucidating the molecular mechanisms underlying its activity. Recombinant RNF32 protein has emerged as a critical tool for these investigations, allowing for in vitro studies to dissect its enzymatic functions and interaction networks. Furthermore, the potential of RNF32 as a therapeutic target in oncology underlines the importance of studying this protein, as it may provide insights into novel treatment strategies. Overall, the investigation of RNF32 and its recombinant forms is essential for advancing our understanding of its biological roles and potential implications in human health and disease.
