Analytical Data
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基因名
CUL1-RBX1
- Application
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别名
Cullin-1; CUL1; Homo sapiens; Human; CUL-1
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种属
Human
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表达系统
Baculovirus
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q13616 (S2-A776)&P62877
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表达区间
Q13616 (S2-A776)&P62877 (M1-H108)
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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
CUL1-RBX1 is a crucial component of the ubiquitin-proteasome system, playing a significant role in cellular protein degradation and regulation of various biological processes. CUL1 (Cullin-1) is a scaffold protein that forms a complex with RBX1 (Ring Box 1), which functions as a ubiquitin ligase. This complex facilitates the attachment of ubiquitin molecules to target proteins, signaling them for degradation by the proteasome. Dysregulation of the CUL1-RBX1 complex has been implicated in various diseases, including cancer, where abnormal protein degradation can lead to uncontrolled cell proliferation and tumor progression. Consequently, studying the CUL1-RBX1 complex is paramount for understanding its roles in cellular homeostasis and its potential as a therapeutic target. Researchers have been increasingly focused on the structural and functional aspects of this complex, employing techniques such as X-ray crystallography and cryo-electron microscopy to elucidate its mechanisms. A deeper understanding of CUL1-RBX1 could provide insights into novel drug developments aimed at modulating its activity, offering new avenues for treating diseases associated with protein homeostasis disruptions.
