Analytical Data
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基因名
RFC3
- Application
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别名
RFC38; Activator 1 38 kDa subunit; Activator 1 subunit 3; Replication factor C 38 kDa subunit
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P40938
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表达区间
Met1~Pro288
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分子量
38kDa
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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
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Protein Description
RFC3, or Replication Factor C3, is a critical component of the DNA replication machinery that plays a significant role in the loading of the proliferating cell nuclear antigen (PCNA) onto DNA. PCNA serves as a sliding clamp that enhances the efficiency and fidelity of DNA polymerases during replication. Understanding RFC3’s structural and functional properties is essential for elucidating the mechanisms of DNA replication, repair, and cell cycle regulation. Dysfunctional RFC3 has been implicated in various diseases, including cancer, highlighting its importance in maintaining genomic stability. Research into RFC3 often focuses on its interactions with other proteins in the replication complex and its regulatory role in cellular processes. By studying RFC3 and its recombination protein function, scientists aim to identify potential therapeutic targets for cancer treatment and develop strategies to modulate its activity. In recent years, advancements in techniques such as cryo-electron microscopy and X-ray crystallography have facilitated detailed structural analyses of RFC3, revealing insights into its conformational changes and interactions at the molecular level. Understanding the dynamics of RFC3 not only enhances our knowledge of fundamental biological processes but also contributes to the broader field of molecular biology and therapeutic development. As research progresses, elucidating the intricate workings of RFC3 may pave the way for innovative approaches to tackle diseases associated with DNA replication errors.
