| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HHIPL1 |
| Uniprot No | Q96JK4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-782aa |
| 氨基酸序列 | HPQCLDFRPPFRPTQPLRLCAQYSDFGCCDEGRDAELTRRFWALASRVDAAEWAACAGYARDLLCQECSPYAAHLYDAEDPFTPLRTVPGLCQDYCLDMWHKCRGLFRHLSTDQELWALEGNLARFCRYLSLDDTDYCFPYLLVNKNLNSNLGHVVADAKGCLQLCLEEVANGLRNPVAMVHARDGTHRFFVAEQVGLVWAYLPDRSRLGKPFLNISRVVLTSPWEGDERGFLGIAFHPSFQHNRRLYVYYSVGIRSSEWIRISEFRVSEDDENAVDHSSERIILEVKEPASNHNGGQLLFGDDGYLYIFTGDGGMAGDPFGTFGNAQNKSALLGKVLRIDVDRKERGLPYGIPPDNPFVGDPAAQPEVYALGVRNMWRCSFDRGDPSSGTGRGRLFCGDVGQNKFEEVDVVERGGNYGWRAREGFECYDRSLCANTSLNDLLPIFAYPHTVGKSVTGGYVYRGCEYPNLNGLYIFGDFMSGRLMSLQENPGTGQWQYSEICMGHGQTCEFPGLINNYYPYIISFGEDEAGELYFMSTGEPSATAPRGVVYKIIDASRRAPPGKCQIQPAQVKIRSRLIPFVPKEKFIPKTRSTPRPTARAPTRAPRRGRPTAAPPAPTPRPARPTQQPGSRRGGGRRRGRLNSASRAFRDGEVRLVRPAGLSSGSGRVEVFVGGRWGTVCDDSWNISGAAVVCRQLGFAYAVRAVKRAEFGQGGSLPILLDDVRCAGWERNLLECQHNGVGTHNCEHDEDAGVVCSHQNPDL |
| 预测分子量 | 90.9 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. |
以下是关于HHIPL1重组蛋白的3篇参考文献示例(文献信息为模拟虚构内容，仅供格式参考)：
1. **文献名称**: *"Expression and functional characterization of recombinant HHIPL1 protein in cardiovascular development"*
**作者**: Zhang Y, et al.
**摘要**: 本研究通过大肠杆菌系统成功表达并纯化了HHIPL1重组蛋白，发现其通过调控Hedgehog信号通路参与小鼠心脏发育，为先天性心脏病机制提供了新见解。
2. **文献名称**: *"Structural analysis of HHIPL1 and its interaction with lipoprotein particles"*
**作者**: Lee S, et al.
**摘要**: 利用X射线晶体学解析HHIPL1重组蛋白结构，揭示其通过特定结构域结合低密度脂蛋白(LDL)，提示其在脂代谢异常相关肝病中的潜在作用。
3. **文献名称**: *"HHIPL1 recombinant protein inhibits fibrosis in a murine model of liver injury"*
**作者**: Gupta R, et al.
**摘要**: 实验证明，外源性HHIPL1重组蛋白能显著减轻小鼠肝纤维化程度，机制涉及TGF-β信号通路抑制，提示其作为抗纤维化治疗候选分子的潜力。
注：以上文献为示例模板，实际研究中请通过PubMed或Web of Science以关键词“HHIPL1 recombinant”检索真实文献。
**Background of HHIPL1 Recombinant Protein**
HHIPL1 (Hedgehog-interacting protein-like 1) is a secreted glycoprotein belonging to the HHIP family, which regulates the Hedgehog (HH) signaling pathway—a critical pathway in embryonic development, tissue homeostasis, and cell differentiation. Structurally, HHIPL1 shares homology with HHIP, a well-characterized antagonist of HH ligands (e.g., Sonic Hedgehog). However, HHIPL1 exhibits distinct expression patterns and functional roles. It is primarily expressed in adult tissues, including the liver, heart, and vasculature, suggesting potential involvement in postnatal physiological or pathological processes.
The recombinant HHIPL1 protein is engineered using molecular cloning techniques, typically expressed in *E. coli* or mammalian cell systems (e.g., HEK293) to ensure proper post-translational modifications. Purification methods, such as affinity chromatography with tags (e.g., His-tag), yield high-purity proteins for research applications.
Functionally, HHIPL1 modulates HH signaling by interacting with HH ligands or receptors, though its precise mechanism remains under investigation. Studies suggest it may act as a context-dependent regulator—either enhancing or inhibiting pathway activity—depending on tissue type or disease state. Its role in pathologies, such as cardiovascular diseases, fibrosis, and cancers, has garnered interest. For example, HHIPL1 deletion in mice exacerbates atherosclerosis, implicating it in vascular protection.
Research applications of HHIPL1 recombinant protein include *in vitro* and *in vivo* studies to dissect its signaling mechanisms, screen therapeutic agents targeting the HH pathway, and develop diagnostic biomarkers. Its potential as a therapeutic target arises from its involvement in diseases driven by dysregulated HH signaling. Further structural and functional studies are essential to clarify its dual regulatory roles and translational relevance.
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