| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | vpl1 |
| Uniprot No | Q9UR19 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-361aa |
| 氨基酸序列 | ATCADGRTTANAACCVLFPILDDIQENLFDGAQCGEEVHESLRLTFHDAIGFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAGDFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILARMSDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLSDVEQACAATPFPALTADPGPVTSVPPVPGS |
| 预测分子量 | 42.0 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VPL1重组蛋白的文献示例(虚构内容，供参考)：
1. **文献名称**: *"Functional analysis of recombinant VPL1 protein in Arabidopsis drought tolerance"*
**作者**: Yamaguchi-Shinozaki, K. et al.
**摘要**: 本研究在大肠杆菌中重组表达了拟南芥VPL1蛋白，证实其通过调控胁迫响应基因的启动子结合活性，增强植物对干旱胁迫的耐受性。
2. **文献名称**: *"Expression and purification of VPL1 recombinant protein for structural studies"*
**作者**: Liu, X. & Wang, Y.
**摘要**: 报道了一种高效的可溶性VPL1重组蛋白表达与纯化方案(使用His标签)，通过X射线晶体学解析其三维结构，揭示其DNA结合域的关键位点。
3. **文献名称**: *"VPL1 recombinant protein interacts with ABA signaling components in vitro"*
**作者**: Chen, Z. et al.
**摘要**: 利用酵母双杂交和体外Pull-down实验，证明重组VPL1蛋白与脱落酸(ABA)信号通路中的转录因子ABF2直接互作，调控种子萌发过程。
注：以上文献为示例，实际研究中建议通过PubMed或Web of Science以“VPL1 recombinant protein”为关键词检索真实文献。
**Background of VPL1 Recombinant Protein**
VPL1 (VASCULAR PLANT ONE-1) is a nuclear-localized transcriptional regulator initially identified in *Arabidopsis thaliana*. It belongs to the B3 domain-containing protein family, which plays critical roles in plant development and stress responses. VPL1 is particularly associated with regulating seed maturation processes, including the accumulation of storage proteins and lipids, by binding to specific DNA sequences in target gene promoters. Its activity is closely linked to the abscisic acid (ABA) signaling pathway, a key hormone mediating plant adaptation to environmental stresses like drought and salinity.
The recombinant VPL1 protein is engineered through molecular cloning, typically expressed in *E. coli* or yeast systems, followed by purification to achieve high homogeneity. This recombinant form retains the functional B3 DNA-binding domain, enabling researchers to study its interaction with gene promoters *in vitro* and dissect its regulatory mechanisms. Its applications span plant molecular biology, including functional studies of seed development, stress adaptation, and genetic engineering to enhance crop resilience.
Research on VPL1 also contributes to understanding the evolutionary conservation of B3 proteins across plant species, offering insights into improving agricultural traits. By leveraging recombinant VPL1. scientists aim to decode complex gene networks governing plant growth and survival, with potential implications for addressing food security challenges in changing climates.
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