| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JUNB |
| Uniprot No | P17275 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-347aa |
| 氨基酸序列 | MCTKMEQPFYHDDSYTATGYGRAPGGLSLHDYKLLKPSLAVNLADPYRSL KAPGARGPGPEGGGGGSYFSGQGSDTGASLKLASSELERLIVPNSNGVIT TTPTPPGQYFYPRGGGSGGGAGGAGGGVTEEQEGFADGFVKALDDLHKMN HVTPPNVSLGATGGPPAGPGGVYAGPEPPPVYTNLSSYSPASASSGGAGA AVGTGSSYPTTTISYLPHAPPFAGGHPAQLGLGRGASTFKEEPQTVPEAR SRDATPPVSPINMEDQERIKVERKRLRNRLAATKCRKRKLERIARLEDKV KTLKAENAGLSSTAGLLREQVAQLKQKVMTHVSNGCQLLLGVKGHAF |
| 预测分子量 | 62 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篇关于JUNB重组蛋白的模拟参考文献(非真实存在，供格式参考)：
1. **《JUNB重组蛋白在炎症反应中的调控机制》**
- 作者：Smith A, et al.
- 摘要：研究通过大肠杆菌表达系统纯化JUNB重组蛋白，揭示其通过调控IL-6和TNF-α的转录在巨噬细胞炎症反应中的关键作用，为炎症性疾病治疗提供新靶点。
2. **《JUNB重组蛋白晶体结构解析及DNA结合特性》**
- 作者：Chen L, et al.
- 摘要：首次报道JUNB重组蛋白的X射线晶体结构，发现其碱性亮氨酸拉链结构域与AP-1位点的特异性结合模式，为设计靶向JUNB的小分子抑制剂奠定结构基础。
3. **《JUNB重组蛋白在皮肤癌中的促增殖功能研究》**
- 作者：Wang Y, et al.
- 摘要：利用真核表达系统制备功能性JUNB重组蛋白，证实其通过激活Cyclin D1通路促进黑色素瘤细胞增殖，敲低JUNB可显著抑制肿瘤生长。
(注：以上文献为示例性质，实际研究中建议通过PubMed或Web of Science检索真实文献)
**Background of JUNB Recombinant Protein**
JUNB, a member of the activator protein-1 (AP-1) transcription factor family, plays a critical role in regulating gene expression involved in cell proliferation, differentiation, and apoptosis. It forms homo- or heterodimers with other AP-1 proteins (e.g., FOS, JUN, or ATF family members) to bind DNA at specific promoter or enhancer regions, modulating transcriptional activity. Structurally, JUNB contains a basic leucine zipper (bZIP) domain essential for dimerization and DNA binding, along with transactivation domains that recruit co-regulators.
The recombinant JUNB protein is engineered through molecular cloning, typically expressed in *E. coli* or mammalian systems, followed by purification to ensure high specificity and activity. Recombinant forms allow researchers to study JUNB’s biochemical properties, interactions, and regulatory mechanisms *in vitro*. They are widely used in electrophoretic mobility shift assays (EMSAs), chromatin immunoprecipitation (ChIP), and functional studies exploring its role in cellular pathways, such as the TGF-β/Smad or MAPK/ERK signaling cascades.
JUNB is implicated in diverse physiological and pathological processes. It acts as a tumor suppressor or promoter depending on context, influencing cell cycle progression (e.g., by regulating cyclin D1) and angiogenesis. Dysregulation of JUNB is linked to cancers, autoimmune diseases, and inflammatory disorders. Recombinant JUNB proteins also serve as antigens for antibody development or tools in drug screening to identify modulators of AP-1 activity.
In summary, JUNB recombinant proteins are vital for dissecting its multifaceted roles in health and disease, offering insights into therapeutic targeting of AP-1-mediated pathways.
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