| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PHLPVI |
| Uniprot No | P43215 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-132aa |
| 氨基酸序列 | MVAMFLAVAVVLGLATSPTAEGGKATTEEQKLIEDVNASFRAAMATTANVPPADKYKTFEAAFTVSSKRNLADAVSKAPQLVPKLDEVYNAAYNAADHAAPEDKYEAFVLHFSEALRIIAGTPEVHAVKPGA |
| 预测分子量 | 13,9 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. |
以下是可能与PHLPP(PH domain leucine-rich repeat protein phosphatase)重组蛋白相关的参考文献示例。若“PHLPVI”存在拼写误差，建议确认名称后进一步检索。
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1. **标题**: "PHLPP dephosphorylates Akt and promotes apoptosis in response to cellular stress"
**作者**: Gao T, et al.
**摘要**: 本研究揭示了PHLPP作为Akt激酶的磷酸酶，通过去磷酸化Akt的Ser473位点抑制其活性，从而促进细胞在应激条件下的凋亡。重组PHLPP蛋白被用于体外酶活实验，证实其直接调控Akt信号通路。
2. **标题**: "Targeting PHLPP1 to enhance insulin signaling using recombinant protein delivery"
**作者**: Chen M, et al.
**摘要**: 作者开发了一种重组PHLPP1蛋白递送系统，证明抑制PHLPP1可增强胰岛素受体底物(IRS)的磷酸化，改善糖尿病模型中的胰岛素敏感性，为代谢疾病治疗提供新策略。
3. **标题**: "PHLPP2 regulates PTEN stability and suppresses tumorigenesis through a phosphatase-independent mechanism"
**作者**: Brognard J, et al.
**摘要**: 研究发现PHLPP2通过结合并稳定PTEN蛋白抑制PI3K/AKT通路，重组PHLPP2蛋白实验表明其功能不依赖磷酸酶活性，为癌症靶向治疗提供新视角。
4. **标题**: "Structural basis of PHLPP substrate recognition"
**作者**: Siesser PM, et al.
**摘要**: 通过晶体结构解析重组PHLPP蛋白与底物的复合物，阐明了其底物选择性的分子机制，为设计小分子抑制剂奠定结构基础。
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**注**：若目标蛋白为“PHLPVI”，可能是拼写误差或特定变体，建议核对名称(如PHLPP1/2、HPV L1蛋白等)或补充关键词(如病毒来源、结构域信息)以获取准确文献。
**Background of PHLPVI Recombinant Protein**
The PHLPVI recombinant protein is a engineered biomolecule designed for specific research or therapeutic applications. While the exact biological origin of "PHLPVI" isn't widely documented in public literature, its nomenclature suggests a fusion or modified structure, potentially involving domains from known proteins or synthetic sequences. Recombinant proteins like PHLPVI are typically produced using expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to enable large-scale, pure, and functional protein synthesis.
Such proteins often serve as tools in molecular biology, drug discovery, or diagnostic assays. For instance, PHLPVI might incorporate functional motifs (e.g., binding domains, enzymatic sites, or epitopes) to study protein interactions, cellular pathways, or immune responses. If linked to disease-related targets, it could aid in understanding mechanisms of pathogenesis or screening therapeutic compounds.
The "PHL" prefix may refer to a conserved domain (e.g., a pleckstrin homology-like region) involved in cellular signaling or membrane interactions, while "PVI" could denote a viral or synthetic component. Tags (e.g., His-tag, FLAG) are commonly added to facilitate purification or detection.
Recombinant proteins like PHLPVI underscore advancements in genetic engineering, enabling tailored designs for precision research. Their applications span vaccine development, structural studies, and biopharmaceuticals, highlighting their versatility in bridging basic science and clinical innovation. Further characterization of PHLPVI would require details on its sequence, target, and experimental context, emphasizing the importance of protein annotation in advancing functional studies.
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