Analytical Data
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基因名
RNF32
- Application
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别名
RNF32; FKSG33; HSD15; RING finger protein 32
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9H0A6
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表达区间
1-362 aa
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氨基酸序列
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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分子量
41.5 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
Related Products
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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.
