| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHLP |
| Uniprot No | Q9CA67 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 44-467aa |
| 氨基酸序列 | AARATPKLSNRKLRVAVIGGGPAGGAAAETLAQGGIETILIERKMDNCKPCGGAIPLCMVGEFNLPLDIIDRRVTKMKMISPSNIAVDIGRTLKEHEYIGMVRREVLDAYLRERAEKSGATVINGLFLKMDHPENWDSPYTLHYTEYDGKTGATGTKKTMEVDAVIGADGANSRVAKSIDAGDYDYAIAFQERIRIPDEKMTYYEDLAEMYVGDDVSPDFYGWVFPKCDHVAVGTGTVTHKGDIKKFQLATRNRAKDKILGGKIIRVEAHPIPEHPRPRRLSKRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKKMIDEGDLRKYLEKWDKTYLPTYRVLDVLQKVFYRSNPAREAFVEMCNDEYVQKMTFDSYLYKRVAPGSPLEDIKLAVNTIGSLVRANALRREIEKLSV |
| 预测分子量 | 63.1 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CHLP重组蛋白的虚构参考文献示例(非真实文献)：
1. **文献名称**：*Expression and Functional Analysis of CHLP Recombinant Protein in Chlorophyll Biosynthesis*
**作者**：Zhang, L. et al.
**摘要**：该研究成功在大肠杆菌中表达并纯化了CHLP重组蛋白，证实其作为叶绿体水解酶的关键作用。实验表明，CHLP通过催化叶绿素前体的水解，影响植物光合作用效率，为作物改良提供理论依据。
2. **文献名称**：*Structural Characterization of CHLP Recombinant Enzyme in Cholesterol Metabolism*
**作者**：Smith, J.R. & Tanaka, M.
**摘要**：通过X射线晶体学解析了CHLP蛋白的三维结构，揭示其与胆固醇酯水解活性相关的活性位点。研究发现，CHLP在低密度脂蛋白代谢中具有调控功能，可能成为心血管疾病的潜在治疗靶点。
3. **文献名称**：*Heterologous Production of CHLP in Yeast for Industrial Applications*
**作者**：Guo, Y. et al.
**摘要**：研究利用毕赤酵母系统高效表达CHLP重组蛋白，优化发酵条件后产量提升3倍。该蛋白展现出高效的酯酶活性，可用于生物柴油生产中的甘油酯水解工艺。
4. **文献名称**：*CRISPR-mediated Overexpression of CHLP Enhances Stress Tolerance in Arabidopsis*
**作者**：Chen, H. & Wang, X.
**摘要**：通过基因编辑技术过表达CHLP蛋白，显著提高了拟南芥的耐盐性和抗氧化能力。蛋白质组学分析表明，CHLP通过调控活性氧代谢通路增强植物逆境适应性。
注：以上内容为示例性虚构，实际研究中请依据具体领域检索真实文献。
CHLP recombinant protein, often derived from the chlorophyll a/b-binding protein (CAB) family or related metabolic enzymes, is a engineered protein produced through recombinant DNA technology. CHLP typically refers to proteins involved in chlorophyll metabolism, photosynthesis, or lipid-associated pathways, depending on the specific biological context. For instance, in photosynthetic organisms, certain CHLP homologs participate in chlorophyll biosynthesis, degradation, or light-harvesting complex assembly. In human or mammalian systems, analogous proteins might be linked to lipid transport or metabolic regulation.
The development of recombinant CHLP aims to enable scalable, high-purity protein production for functional studies and biotechnological applications. Using expression systems like *E. coli*, yeast, or mammalian cells, researchers clone the CHLP gene into expression vectors, optimize codon usage for the host organism, and purify the protein via affinity tags (e.g., His-tag). This approach overcomes limitations in isolating native CHLP from natural sources, which often suffers from low yield or contamination.
Recombinant CHLP proteins are critical tools for investigating chlorophyll-related pathways in plants, algae, or photosynthetic bacteria, aiding research on crop stress responses or biofuel production. In biomedical fields, CHLP variants may serve as antigens for antibody development, enzyme activity assays, or models to study lipid metabolism disorders. Their structural analysis via X-ray crystallography or cryo-EM often relies on recombinant versions due to sample homogeneity requirements. Additionally, engineered CHLP proteins with modified stability or catalytic activity have potential in industrial biocatalysis or green chemistry. Ongoing research focuses on optimizing expression conditions and functional validation to expand its utility in agriculture, energy, and therapeutics.
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