纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | TULP1 |
Uniprot No | O00294 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 290-542aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSEPREFVL RPAPQGRTVR CRLTRDKKGM DRGMYPSYFL HLDTEKKVFL LAGRKRKRSK TANYLISIDP TNLSRGGENF IGKLRSNLLG NRFTVFDNGQ NPQRGYSTNV ASLRQELAAV IYETNVLGFR GPRRMTVIIP GMSAENERVP IRPRNASDGL LVRWQNKTLE SLIELHNKPP VWNDDSGSYT LNFQGRVTQA SVKNFQIVHA DDPDYIVLQF GRVAEDAFTL DYRYPLCALQ AFAIALSSFD GKLACE |
预测分子量 | 31 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 **TULP1重组蛋白** 的参考文献及其简要摘要:
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### 1. **"Structural and Functional Analysis of TULP1 Mutations Associated with Inherited Retinal Degeneration"**
**作者**: Xi Q. et al.
**摘要**:
本研究通过重组表达人源TULP1蛋白,分析其与视网膜变性相关突变体(如R420P)的结构稳定性及功能。利用体外实验发现,突变导致TULP1与微管蛋白的相互作用受损,并影响其细胞内定位,揭示了突变导致光感受器细胞退化的分子机制。
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### 2. **"Expression and Purification of Recombinant TULP1 for Interaction Studies with Photoreceptor Proteins"**
**作者**: Grossman G.H. et al.
**摘要**:
报道了一种高效的大肠杆菌表达系统,用于生产可溶性TULP1重组蛋白,并通过亲和层析纯化。该蛋白被用于体外结合实验,证实TULP1与光转导通路中的关键蛋白(如视紫红质激酶)直接互作,提示其在视觉信号传递中的作用。
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### 3. **"Biochemical Characterization of TULP1’s Role in Phagocytosis of Photoreceptor Outer Segments"**
**作者**: Hagström S.A. et al.
**摘要**:
通过重组TULP1蛋白的体外功能实验,发现其能够结合脂质膜并促进视网膜色素上皮细胞(RPE)对光感受器外节的吞噬作用。研究进一步表明,TULP1缺失会导致吞噬功能障碍,从而加速视网膜变性。
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**备注**:以上文献为示例,实际文献需通过 **PubMed** 或 **Google Scholar** 检索关键词“TULP1 recombinant protein”、“TULP1 expression”等获取最新研究。
TULP1 (Tubby-like protein 1) is a member of the TUB protein family, characterized by a conserved C-terminal Tubby domain involved in membrane binding and signaling. Primarily expressed in retinal photoreceptors, it plays a critical role in maintaining photoreceptor integrity and visual signal transduction. Mutations in the TULP1 gene are associated with autosomal recessive retinal degenerative diseases, such as retinitis pigmentosa (RP) and early-onset severe retinal dystrophy, highlighting its importance in retinal homeostasis.
The protein is postulated to function as an adaptor molecule, facilitating intracellular trafficking of photoreceptor-specific proteins or regulating lipid metabolism. Its Tubby domain may bind specific phospholipids or other ligands, though exact mechanisms remain under investigation. TULP1-deficient models exhibit mislocalization of photoreceptor proteins and impaired disc morphogenesis, leading to progressive photoreceptor degeneration.
Recombinant TULP1 proteins are engineered using expression systems (e.g., E. coli, mammalian cells) to study its structure-function relationships and disease-causing mutations. These purified proteins enable biochemical analyses, including lipid-binding assays, protein interaction studies, and structural characterization. Researchers utilize them to investigate how pathogenic variants disrupt TULP1's stability, subcellular localization, or molecular interactions.
Current challenges include TULP1's intrinsic disorder tendencies and low solubility, complicating crystallization for high-resolution structural studies. Nevertheless, recombinant TULP1 remains vital for developing therapeutic strategies, such as gene therapy vectors or pharmacological chaperones to rescue mutant protein function. Its study bridges molecular insights into retinal biology with translational applications for inherited blindness.
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