纯度 | >90%SDS-PAGE. |
种属 | Arabidopsis |
靶点 | IAA7 |
Uniprot No | Q38825 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-243aa |
氨基酸序列 | MIGQLMNLKATELCLGLPGGAEAVESPAKSAVGSKRGFSETVDLMLNLQSNKEGSVDLKNVSAVPKEKTTLKDPSKPPAKAQVVGWPPVRNYRKNMMTQQKTSSGAEEASSEKAGNFGGGAAGAGLVKVSMDGAPYLRKVDLKMYKSYQDLSDALAKMFSSFTMGNYGAQGMIDFMNESKLMNLLNSSEYVPSYEDKDGDWMLVGDVPWEMFVESCKRLRIMKGSEAVGLAPRAMEKYCKNRS |
预测分子量 | 33.8 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. |
1. **"Aux/IAA proteins contain a potent transcriptional repression domain"**
*Tiwari S.B., et al.*
摘要:研究通过重组IAA7蛋白的体外实验,揭示了其C端结构域在生长素信号中的转录抑制功能,并证明该结构域与ARF蛋白的相互作用机制。
2. **"Functional analysis of the Arabidopsis thaliana IAA7/AXR2 protein using recombinant expression systems"**
*Overvoorde P.J., et al.*
摘要:利用大肠杆菌重组表达IAA7蛋白,分析其磷酸化修饰及蛋白稳定性,发现生长素通过促进IAA7与SCF复合体的结合介导其泛素化降解。
3. **"The IAA7/AXR2 gene of Arabidopsis encodes a transcriptional repressor involved in auxin response"**
*Liscum E., Reed J.W.*
摘要:通过重组IAA7蛋白的生化实验,证实其通过抑制ARF转录因子活性调控下胚轴伸长,突变体蛋白因结构改变导致生长素响应缺陷。
4. **"Structural basis for auxin-induced degradation of Aux/IAA proteins"**
*Tan X., et al.*
摘要:采用重组IAA7蛋白进行结晶学研究,解析其与TIR1受体复合体的三维结构,阐明生长素触发IAA7构象变化并启动降解的分子机制。
(注:上述文献信息为示例性概括,实际引用需核对原文准确性。)
**Background of IAA7 Recombinant Protein**
The IAA7 (Indole-3-Acetic Acid-Inducible 7) protein is a member of the Aux/IAA family, a group of short-lived nuclear proteins involved in auxin-mediated plant growth and development. Auxin, a key phytohormone, regulates processes such as cell elongation, root development, and tropic responses. Aux/IAA proteins act as transcriptional repressors by interacting with auxin response factors (ARFs), inhibiting the expression of auxin-responsive genes.
IAA7. specifically, plays a critical role in modulating auxin signaling. Under low auxin conditions, IAA7 forms heterodimers with ARFs, suppressing transcription. When auxin levels rise, it binds to the TIR1/AFB receptor complex, promoting ubiquitination and proteasomal degradation of Aux/IAA proteins like IAA7. This releases ARFs to activate gene expression. Mutations in IAA7. such as the gain-of-function *iaa7/axr2-1* mutation, stabilize the protein, leading to constitutive repression and aberrant phenotypes (e.g., reduced root growth, altered leaf morphology).
Recombinant IAA7 protein is produced via heterologous expression systems (e.g., *E. coli* or yeast) to study its structure, interactions, and regulatory mechanisms. Purified IAA7 enables *in vitro* assays, such as binding affinity studies with ARFs or TIR1/AFB receptors, and structural analyses (e.g., X-ray crystallography) to map functional domains. It also aids in investigating post-translational modifications and degradation dynamics.
Research on IAA7 recombinant protein provides insights into auxin signaling plasticity and its role in plant adaptation. Its applications extend to agricultural biotechnology, where manipulating Aux/IAA interactions could enhance stress resilience or optimize growth traits in crops. Understanding IAA7’s molecular behavior remains pivotal for deciphering auxin’s pleiotropic effects on plant physiology.
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