| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VLDLR |
| Uniprot No | P98155 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-769aa |
| 氨基酸序列 | GRKAKCEPSQFQCTNGRCITLLWKCDGDEDCVDGSDEKNCVKKTCAESDF VCNNGQCVPSRWKCDGDPDCEDGSDESPEQCHMRTCRIHEISCGAHSTQC IPVSWRCDGENDCDSGEDEENCGNITCSPDEFTCSSGRCISRNFVCNGQD DCSDGSDELDCAPPTCGAHEFQCSTSSCIPISWVCDDDADCSDQSDESLE QCGRQPVIHTKCPASEIQCGSGECIHKKWRCDGDPDCKDGSDEVNCPSRT CRPDQFECEDGSCIHGSRQCNGIRDCVDGSDEVNCKNVNQCLGPGKFKCR SGECIDISKVCNQEQDCRDWSDEPLKECHINECLVNNGGCSHICKDLVIG YECDCAAGFELIDRKTCGDIDECQNPGICSQICINLKGGYKCECSRGYQM DLATGVCKAVGKEPSLIFTNRRDIRKIGLERKEYIQLVEQLRNTVALDAD IAAQKLFWADLSQKAIFSASIDDKVGRHVKMIDNVYNPAAIAVDWVYKTI YWTDAASKTISVATLDGTKRKFLFNSDLREPASIAVDPLSGFVYWSDWGE PAKIEKAGMNGFDRRPLVTADIQWPNGITLDLIKSRLYWLDSKLHMLSSV DLNGQDRRIVLKSLEFLAHPLALTIFEDRVYWIDGENEAVYGANKFTGSE LATLVNNLNDAQDIIVYHELVQPSGKNWCEEDMENGGCEYLCLPAPQIND HSPKYTCSCPSGYNVEENGRDCQSTATTVTYSETKDTNTTEIS |
| 预测分子量 | 86 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VLDLR重组蛋白的3篇参考文献示例(文献信息为模拟概括，仅供参考)：
1. **文献名称**：*"Expression and functional characterization of recombinant human VLDLR: Role in cellular lipid uptake"*
**作者**：Smith A, et al.
**摘要**：研究通过哺乳动物细胞表达系统成功制备重组人VLDLR蛋白，证实其在介导脂蛋白颗粒(如β-VLDL)内吞中的作用，并分析其与配体结合的动力学特性。
2. **文献名称**：*"Structural insights into VLDLR ligand binding domains through recombinant protein crystallization"*
**作者**：Chen L, et al.
**摘要**：利用昆虫细胞表达系统获得VLDLR胞外结构域的重组蛋白，通过X射线晶体学解析其三维结构，揭示其与RAP蛋白(受体相关蛋白)相互作用的分子机制。
3. **文献名称**：*"VLDLR mutations disrupt Reelin signaling: Functional validation using recombinant receptor assays"*
**作者**：Nakamura K, et al.
**摘要**：通过体外重组VLDLR蛋白实验，验证小脑发育相关基因突变对Reelin信号通路的影响，证明特定突变导致受体磷酸化及下游信号传导异常。
(注：以上文献为示例性内容，实际引用需查询PubMed、Google Scholar等数据库获取真实信息。)
**Background of VLDLR Recombinant Protein**
The very-low-density lipoprotein receptor (VLDLR) is a cell-surface protein belonging to the low-density lipoprotein receptor (LDLR) family. It plays a critical role in lipid metabolism and cellular signaling by mediating the uptake of triglyceride-rich lipoproteins, such as VLDL and remnant chylomicrons, into cells. Structurally, VLDLR consists of ligand-binding domains, epidermal growth factor (EGF)-like repeats, a transmembrane region, and a cytoplasmic tail. Unlike LDLR, VLDLR lacks the O-linked sugar domain and is predominantly expressed in peripheral tissues (e.g., heart, muscle, adipose) and the brain, where it supports neuronal migration and synaptic plasticity during development.
VLDLR recombinant protein is engineered *in vitro* using expression systems like mammalian cells (e.g., HEK293. CHO) or insect cells to ensure proper post-translational modifications, such as glycosylation. This recombinant form retains the functional domains required for ligand binding and intracellular trafficking, enabling studies on its interaction with apolipoproteins (e.g., ApoE, ApoB) or signaling molecules like Reelin, a key regulator of brain development. Researchers utilize VLDLR recombinant protein to investigate lipid homeostasis, neurodevelopmental disorders, and metabolic diseases. Mutations in *VLDLR* are linked to autosomal recessive cerebellar ataxia, underscoring its neurological importance.
In drug discovery, VLDLR recombinant protein aids in screening compounds targeting dyslipidemia or neurodegenerative conditions. Its application extends to structural biology (e.g., crystallography) and diagnostic assays for VLDLR-related pathologies. Overall, VLDLR recombinant protein serves as a vital tool for unraveling the receptor’s physiological roles and therapeutic potential.
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