| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HDLBP |
| Uniprot No | Q00341 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1060-1268aa |
| 氨基酸序列 | DPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNQPQDQITITGYEKNTEAARDAILRIVGELEQMVSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHILNLEEEYLADVVDSEALQVYMKPPAHEEAKAPSRGFVVRDAPWTASSSEKAPDMSSSEEFPSFGAQVAPKTLPWGPKR |
| 预测分子量 | 30.1 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HDLBP重组蛋白的3篇模拟参考文献示例(文献信息为虚构，仅供格式参考)：
1. **文献名称**: "Recombinant HDLBP Expression and Its Role in Cholesterol Transport"
**作者**: Smith A, et al.
**摘要**: 研究通过大肠杆菌系统成功表达并纯化HDLBP重组蛋白，证实其在体外可特异性结合高密度脂蛋白(HDL)，并调控胆固醇逆向转运过程，为脂代谢疾病治疗提供潜在靶点。
2. **文献名称**: "Structural Characterization of HDLBP/Vigilin by Cryo-EM"
**作者**: Chen L, et al.
**摘要**: 利用冷冻电镜解析HDLBP重组蛋白的三维结构，揭示其多个KH结构域的空间排列，阐明了HDLBP与RNA及脂蛋白相互作用的分子机制。
3. **文献名称**: "HDLBP Promotes Cancer Metastasis via Stabilizing Oncogenic mRNAs"
**作者**: Wang Y, et al.
**摘要**: 通过哺乳动物细胞表达重组HDLBP，发现其通过结合并稳定促癌基因mRNA(如MMP9)，增强肿瘤细胞侵袭能力，提示HDLBP可作为癌症治疗的干预靶点。
(注：以上文献为模拟内容，实际研究中请通过PubMed、Google Scholar等平台检索真实文献。)
**Background of HDLBP Recombinant Protein**
HDLBP (High-Density Lipoprotein Binding Protein), also known as vigilin, is a multifunctional RNA-binding protein implicated in diverse cellular processes, including cholesterol metabolism, RNA stabilization, and translational regulation. It was initially identified through its interaction with high-density lipoprotein (HDL) particles, though subsequent studies revealed broader roles in cellular homeostasis. Structurally, HDLBP contains 14 tandemly arranged K-homology (KH) domains, which facilitate RNA binding and protein-protein interactions, enabling its participation in post-transcriptional gene regulation.
Recombinant HDLBP protein is engineered using molecular cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. Purification methods often involve affinity tags (e.g., His-tag) for efficient isolation. This recombinant form retains the functional domains of native HDLBP, making it valuable for *in vitro* studies to dissect its molecular mechanisms, such as RNA binding specificity, interactions with lipoproteins, or roles in stress granule formation.
Research highlights HDLBP's involvement in diseases like atherosclerosis, where it modulates cholesterol efflux, and neurodegenerative disorders, including Alzheimer’s disease, due to its impact on mRNA stability. Dysregulation of HDLBP has also been linked to cancer progression, as it influences oncogene expression and metastasis. Recombinant HDLBP serves as a critical tool for structural analysis, inhibitor screening, and functional assays, aiding therapeutic development. Its versatility underscores its importance in both basic research and translational applications, bridging gaps in understanding RNA-protein interactions and metabolic disease pathways.
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