| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JUN |
| Uniprot No | P05412 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-131aa |
| 氨基酸序列 | MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF |
| 预测分子量 | 41.3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 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. |
以下是3条与JUN重组蛋白相关的文献示例(内容为模拟概括，非真实文献)：
1. **"Functional characterization of recombinant c-Jun protein in AP-1 signaling pathway"**
- 作者：Zhang L, et al.
- 摘要：通过大肠杆菌表达系统纯化重组c-Jun蛋白，验证其与DNA结合活性及在AP-1通路中对靶基因转录的调控作用，证实其参与细胞应激反应的分子机制。
2. **"High-yield production of JUN recombinant protein using baculovirus-insect cell system"**
- 作者：Sato K, et al.
- 摘要：利用杆状病毒-昆虫细胞系统高效表达JUN重组蛋白，优化纯化工艺并用于体外激酶实验，揭示JUN磷酸化位点对肿瘤细胞增殖的影响。
3. **"Structural analysis of recombinant JUN-FOS heterodimer by cryo-EM"**
- 作者：Müller R, et al.
- 摘要：通过冷冻电镜解析重组JUN-FOS异源二聚体的三维结构，阐明其与DNA结合域的关键氨基酸残基，为设计靶向AP-1的小分子抑制剂提供结构基础。
注：以上为示例性内容，实际文献需通过PubMed或Web of Science以关键词“JUN recombinant protein”或“c-Jun expression”检索获取。
The JUN recombinant protein is derived from the c-Jun proto-oncogene, a key component of the activator protein-1 (AP-1) transcription factor family. c-Jun, first identified as a viral oncogene homolog (v-Jun), plays a central role in regulating gene expression linked to cell proliferation, differentiation, apoptosis, and stress responses. Structurally, JUN contains a basic leucine zipper (bZIP) domain that facilitates dimerization with other AP-1 members (e.g., FOS, ATF) and binds to specific DNA sequences (TRE/CRE motifs) to modulate transcriptional activity. Its function is tightly regulated by post-translational modifications, such as phosphorylation by kinases like JNK (c-Jun N-terminal kinase), which activates AP-1-dependent gene programs in response to cytokines, growth factors, or cellular stressors.
Recombinant JUN proteins are typically produced using expression systems like *E. coli* or mammalian cell cultures, followed by purification via affinity chromatography. These engineered proteins retain functional domains critical for studying AP-1 signaling mechanisms, including dimerization, DNA binding, and interactions with co-regulators. Researchers employ JUN recombinant proteins in diverse applications: dissecting MAPK/AP-1 pathway dynamics, modeling diseases (e.g., cancer, inflammation), and screening compounds that modulate AP-1 activity for therapeutic development. Additionally, structural studies using recombinant JUN have advanced understanding of its interaction interfaces, aiding drug design targeting aberrant AP-1 activity in oncology and autoimmune disorders. As a versatile tool, JUN recombinant protein bridges molecular biology and translational research, offering insights into cellular decision-making and therapeutic targeting of AP-1-driven pathologies.
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