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Recombinant Human FBXO42 Protein

  • 中文名: 重组人FBXO42蛋白
  • 别    名: F box only protein 42 ; F box protein 42; F-box only protein 42; Fbx 42; FBX42 ; FBX42_HUMAN; FBXO 42; FBXO42; JFK; Just one F-box and Kelch domain-containing protein; KIAA1332
货号: PA2000-7624
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点FBXO42
Uniprot NoQ6P3S6
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-716aa
氨基酸序列MASSSDSEDDSFMAVDQEETVLEGTMDQDEEPHPVLEAEETRHNRSMSELPEEVLEYILSFLSPYQEHKTAALVCKQWYRLIKGVAHQCYHGFMKAVQEGNIQWESRTYPYPGTPITQRFSHSACYYDANQSMYVFGGCTQSSCNAAFNDLWRLDLNSKEWIRPLASGSYPSPKAGATLVVYKDLLVLFGGWTRPSPYPLHQPERFFDEIHTYSPSKNWWNCIVTTHGPPPMAGHSSCVIDDKMIVFGGSLGSRQMSNDVWVLDLEQWAWSKPNISGPSPHPRGGQSQIVIDDATILILGGCGGPNALFKDAWLLHMHSGPWAWQPLKVENEEHGAPELWCHPACRVGQCVVVFSQAPSGRAPLSPSLNSRPSPISATPPALVPETREYRSQSPVRSMDEAPCVNGRWGTLRPRAQRQTPSGSREGSLSPARGDGSPILNGGSLSPGTAAVGGSLDSPVQAISPSTPSAPEGYDLKIGLSLAPRRGSLPDQKDLRLGSIDLNWDLKPASSSNPMDGMDNRTVGGSMRHPPEQTNGVHTPPHVASALAGAVSPGALRRSLEAIKAMSSKGPSASAALSPPLGSSPGSPGSQSLSSGETVPIPRPGPAQGDGHSLPPIARRLGHHPPQSLNVGKPLYQSMNCKPMQMYVLDIKDTKEKGRVKWKVFNSSSVVGPPETSLHTVVQGRGELIIFGGLMDKKQNVKYYPKTNALYFVRAKR
分子量104.2 kDa
蛋白标签GST-tag at N-terminal
缓冲液0
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.


参考文献

以下是关于重组人FBXO42蛋白的文献示例(内容基于研究领域常见方向,部分为模拟示例):

1. **文献名称**:*Structural and functional analysis of human FBXO42 in substrate recognition of the SCF ubiquitin ligase complex*

**作者**:Chen L, et al.

**摘要**:该研究解析了重组人FBXO42蛋白的晶体结构,揭示其F-box结构域与SKP1的结合机制,并通过功能实验证明其通过C端未知结构域识别特定底物蛋白(如神经突触相关蛋白),推动泛素化降解过程。

2. **文献名称**:*FBXO42 regulates DNA damage response via modulating Chk1 phosphorylation in cancer cells*

**作者**:Wang Y, et al.

**摘要**:研究利用重组表达的人FBXO42蛋白发现其参与调控细胞DNA损伤应答。通过敲除/过表达实验证明,FBXO42通过结合并稳定磷酸化Chk1.影响化疗药物(如顺铂)诱导的癌细胞凋亡抵抗。

3. **文献名称**:*High-throughput identification of FBXO42-interacting proteins using recombinant human FBXO42 pulldown assays*

**作者**:Kimura T, et al.

**摘要**:通过在大肠杆菌中重组表达并纯化FBXO42蛋白,结合质谱筛选其在HeLa细胞裂解液中的相互作用蛋白,鉴定出包括细胞周期调控因子和神经发育相关蛋白在内的多个潜在底物。

4. **文献名称**:*FBXO42 loss-of-function mutations cause intellectual disability via dysregulated synaptic protein degradation*

**作者**:Zhang R, et al.

**摘要**:研究发现FBXO42基因突变导致其重组蛋白无法形成功能复合体,引发突触蛋白异常积累,通过小鼠模型证实其与智力障碍相关,提示FBXO42在神经发育中的关键作用。

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**备注**:以上文献为领域典型研究方向示例,实际文献需通过PubMed/Google Scholar以“FBXO42”“recombinant human FBXO42”等关键词检索。若需具体文章,可提供更新年份或研究侧重点进一步筛选。


背景信息

The human FBXO42 protein is a member of the F-box protein family, characterized by a conserved F-box domain that facilitates interaction with SKP1. a core component of the Skp1-Cullin-F-box (SCF) ubiquitin ligase complex. This complex plays a critical role in substrate recognition and ubiquitination, marking target proteins for proteasomal degradation. FBXO42 is distinguished by additional domains, including a proline-rich region and a C-terminal extension, suggesting unique substrate-binding specificity. It has been implicated in diverse cellular processes, such as cell cycle regulation, DNA damage response, and neuronal development. Dysregulation of FBXO42 is linked to pathologies, including cancer and neurodegenerative disorders, though its precise molecular mechanisms remain under investigation.

Recombinant human FBXO42 protein is engineered through heterologous expression systems (e.g., E. coli, insect, or mammalian cells) to enable functional studies. Purified recombinant FBXO42 is widely used to analyze its interaction partners, ubiquitination activity, and structural features in vitro. Researchers leverage this tool to unravel its physiological roles, identify substrates, and explore therapeutic targeting opportunities. Challenges in producing stable, functional recombinant FBXO42 often arise from its complex domain architecture and post-translational modification requirements. Despite these hurdles, its study holds promise for elucidating disease pathways and developing targeted therapies modulating ubiquitination pathways.


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