| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CCD4 |
| Uniprot No | O49675 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-595aa |
| 氨基酸序列 | MDSVSSSSFLSSTFSLHHSLLRRRSSSPTLLRINSAVVEERSPITNPSDNNDRRNKPKTLHNRTNHTLVSSPPKLRPEMTLATALFTTVEDVINTFIDPPSRPSVDPKHVLSDNFAPVLDELPPTDCEIIHGTLPLSLNGAYIRNGPNPQFLPRGPYHLFDGDGMLHAIKIHNGKATLCSRYVKTYKYNVEKQTGAPVMPNVFSGFNGVTASVARGALTAARVLTGQYNPVNGIGLANTSLAFFSNRLFALGESDLPYAVRLTESGDIETIGRYDFDGKLAMSMTAHPKTDPITGETFAFRYGPVPPFLTYFRFDSAGKKQRDVPIFSMTSPSFLHDFAITKRHAIFAEIQLGMRMNMLDLVLEGGSPVGTDNGKTPRLGVIPKYAGDESEMKWFEVPGFNIIHAINAWDEDDGNSVVLIAPNIMSIEHTLERMDLVHALVEKVKIDLVTGIVRRHPISARNLDFAVINPAFLGRCSRYVYAAIGDPMPKISGVVKLDVSKGDRDDCTVARRMYGSGCYGGEPFFVARDPGNPEAEEDDGYVVTYVHDEVTGESKFLVMDAKSPELEIVAAVRLPRRVPYGFHGLFVKESDLNKL |
| 预测分子量 | 65,6 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CCD4重组蛋白的3篇参考文献，涵盖其功能、表达及应用研究：
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1. **文献名称**：*Carotenoid cleavage dioxygenase (CmCCD4a) contributes to white color formation in chrysanthemum petals*
**作者**：Ohmiya, A., Kishimoto, S., Aida, R., Yoshioka, S., Sumitomo, K.
**摘要**：该研究通过在大肠杆菌中重组表达菊花CmCCD4a蛋白，证实其能够催化类胡萝卜素分解为无色产物，揭示了其在花瓣颜色褪白中的关键作用，为花色改良提供了理论依据。
2. **文献名称**：*The role of carotenoid cleavage dioxygenase (CCD4) in peach fruit pigmentation*
**作者**：Brandi, F., Bar, E., Mourgues, F., et al.
**摘要**：研究通过原核系统表达并纯化桃CCD4重组蛋白，发现其特异性裂解β-胡萝卜素和叶黄素，阐明了其在果肉颜色由黄转白过程中的分子机制。
3. **文献名称**：*Functional characterization of Crocus CCD4 in apocarotenoid biosynthesis*
**作者**：Rubio-Moraga, A., Ahrazem, O., Rambla, J.L., et al.
**摘要**：利用酵母体系重组表达番红花CCD4蛋白，证明其催化玉米黄质分解生成藏红花素前体，为天然色素生物合成途径的酶学基础提供了新见解。
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如需更近期文献，建议通过PubMed或Web of Science以“CCD4 recombinant protein”为关键词检索最新研究进展。
CCD4 (Carotenoid Cleavage Dioxygenase 4) is a key enzyme involved in the oxidative cleavage of carotenoids, a class of pigments critical for plant coloration, photosynthesis, and signaling. It belongs to the CCD protein family, which catalyzes the breakdown of carotenoids into apocarotenoids—compounds with diverse biological roles, including aroma, flavor, and hormone precursors. CCD4 is particularly notable for its role in determining flower and fruit pigmentation. For example, in plants like chrysanthemums, roses, and peaches, CCD4 activity directly influences color intensity by degrading carotenoids such as β-carotene and lutein, thereby reducing yellow/orange hues and contributing to white or pale pigmentation.
Recombinant CCD4 proteins are engineered versions of this enzyme, typically produced in heterologous expression systems like *E. coli* or yeast. These systems allow large-scale production of CCD4 for research and industrial applications. The recombinant protein retains the enzymatic activity of its native counterpart, enabling studies on substrate specificity, catalytic mechanisms, and structure-function relationships. Its crystal structure often reveals conserved features of CCD enzymes, including a hydrophobic substrate-binding pocket and iron-binding motifs essential for dioxygenase activity.
Applications of recombinant CCD4 span agriculture and biotechnology. In horticulture, modulating CCD4 expression or activity through genetic engineering can alter flower/fruit colors, enhancing commercial value. It also holds potential in producing apocarotenoids for fragrances, food additives, or pharmaceuticals. Additionally, studying CCD4 sheds light on carotenoid metabolism pathways, aiding efforts to improve crop nutritional profiles or stress resilience. Despite its utility, challenges remain in optimizing stability and catalytic efficiency in recombinant forms, driving ongoing research into protein engineering and expression strategies.
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