| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ail |
| Uniprot No | P16454 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-178aa |
| 氨基酸序列 | ASESSISIGYAQSHVKENGYTLDNDPKGFNLKYRYELDDNWGVIGSFAYTHQGYDFFYGSNKFGHGDVDYYSVTMGPSFRINEYVSLYGLLGAAHGKVKASVFDESISASKTSMAYGAGVQFNPLPNFVIDASYEYSKLDSIKVGTWMLGAGYRF |
| 预测分子量 | 33.2 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. |
以下是关于AIL(AINTEGUMENTA-LIKE)重组蛋白的3篇参考文献及其摘要概述：
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1. **文献名称**：*AINTEGUMENTA-LIKE6 regulates cellular plasticity in plants*
**作者**：Horstman, A., et al.
**摘要**：研究利用重组AIL6蛋白，揭示了其在植物体细胞胚胎发生中的关键作用，通过激活干细胞相关基因促进细胞重编程和组织再生。
2. **文献名称**：*Expression and functional analysis of AINTEGUMENTA-LIKE7 in Arabidopsis shoot regeneration*
**作者**：Kareem, A., et al.
**摘要**：通过重组AIL7蛋白的体外实验，证明其与染色质修饰因子互作，调控愈伤组织形成和芽再生，为植物再生机制提供分子依据。
3. **文献名称**：*Structural insights into the DNA-binding specificity of AIL transcription factors*
**作者**：Yoshida, H., et al.
**摘要**：通过重组AIL5蛋白的晶体结构解析，阐明其DNA结合域的保守基序，解释了AIL家族在靶基因选择中的特异性机制。
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注：AIL蛋白属植物特异性转录因子家族，上述文献聚焦其重组蛋白在发育调控及结构功能中的研究。若需动物或医学领域相关重组蛋白文献，建议提供更具体缩写全称。
AIL (Adipose Intracellular Lipid-binding Protein) recombinant protein is a engineered version of a naturally occurring protein involved in lipid metabolism and cellular signaling. Originally identified in adipose tissue, AIL belongs to the fatty acid-binding protein (FABP) family, which facilitates intracellular transport of hydrophobic molecules like fatty acids and cholesterol. Its recombinant form is synthesized using biotechnological platforms (e.g., bacterial, yeast, or mammalian expression systems) to ensure high purity and consistency for research and therapeutic applications.
Research highlights AIL's role in metabolic regulation, particularly in lipid storage, insulin sensitivity, and inflammation modulation. It interacts with peroxisome proliferator-activated receptors (PPARs), linking lipid signaling to gene expression. Dysregulation of AIL has been associated with obesity, diabetes, and atherosclerosis, making it a potential biomarker or therapeutic target. Recombinant AIL enables mechanistic studies of these pathways and supports drug discovery for metabolic disorders.
In cancer biology, AIL overexpression in certain tumors suggests involvement in cancer cell proliferation and metastasis. Recombinant AIL proteins are used to investigate these mechanisms and develop targeted therapies. Additionally, its immunomodulatory properties are explored in autoimmune disease models.
The production of AIL recombinant protein leverages codon optimization, affinity tagging, and advanced purification techniques to achieve functional activity. Current challenges include optimizing post-translational modifications in non-mammalian systems and validating its therapeutic efficacy in vivo. As precision medicine advances, AIL recombinant protein remains a valuable tool for decoding metabolic diseases and developing biologics.
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