纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LHPP |
Uniprot No | Q9H008 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-270aa |
氨基酸序列 | MRGSHHHHHP WYASMTGGQQ MGRDLYDDDD KDRWGSHMAP WGKRLAGVRG VLLDISGVLY DSGAGGGTAI AGSVEAVARL KRSRLKVRFC TNESQKSRAE LVGQLQRLGF DISEQEVTAP APAACQILKE QGLRPYLLIH DGVRSEFDQI DTSNPNCVVI ADAGESFSYQ NMNNAFQVLM ELEKPVLISL GKGRYYKETS GLMLDVGPYM KALEYACGIK AEVVGKPSPE FFKSALQAIG VEAHQAVMIG DDIVGDVGGA QRCGMRALQV RTGKFRPSDE HHPEVKADGY VDNLAEAVDL LLQHADK |
预测分子量 | 34 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LHPP重组蛋白的3篇代表性文献概览:
1. **《LHPP suppresses hepatocellular carcinoma progression by regulating p53-mediated apoptosis》**
- 作者:Kumar, A. et al. (2017)
- 摘要:研究通过重组LHPP蛋白验证其抑癌功能,发现其通过激活p53信号通路诱导肝癌细胞凋亡并抑制肿瘤生长。
2. **《Recombinant LHPP protein inhibits cell proliferation via PI3K/AKT pathway in colorectal cancer》**
- 作者:Zhang, Y. et al. (2019)
- 摘要:利用大肠癌细胞系证实重组LHPP蛋白通过抑制PI3K/AKT通路降低细胞增殖和迁移能力。
3. **《Purification and enzymatic characterization of human LHPP phosphatase domain》**
- 作者:Chen, L. et al. (2020)
- 摘要:报道了重组LHPP磷酸酶结构域的纯化方法,并鉴定其特异性水解组氨酸磷酸化的酶活性,为功能研究提供基础。
4. **《LHPP overexpression attenuates stress-induced depressive behaviors in mice》**
- 作者:Wang, Q. et al. (2021)
- 摘要:通过脑内注射重组LHPP蛋白,发现其通过调节神经元突触可塑性改善小鼠抑郁样行为。
注:以上为模拟文献,实际研究中建议通过PubMed或Web of Science以“LHPP recombinant protein”为关键词检索最新论文。
**Background of LHPP Recombinant Protein**
LHPP (phospholysine phosphohistidine inorganic pyrophosphate phosphatase) is a phosphatase enzyme implicated in diverse cellular processes, including nucleotide metabolism, energy homeostasis, and tumor suppression. Initially identified through genomic studies, LHPP catalyzes the hydrolysis of phospholysine and phosphohistidine residues, as well as inorganic pyrophosphate, playing a regulatory role in phosphorylation-dependent signaling pathways. Structurally, it belongs to the histidine phosphatase superfamily, characterized by conserved catalytic domains critical for its enzymatic activity.
Research has highlighted LHPP's association with human diseases, particularly cancer. Studies reveal that LHPP expression is significantly downregulated in hepatocellular carcinoma, gastric cancer, and other malignancies, suggesting its role as a tumor suppressor. Loss of LHPP correlates with dysregulated cellular proliferation, metabolic reprogramming, and enhanced tumor aggressiveness, potentially due to impaired dephosphorylation of oncogenic substrates or disrupted nucleotide pool balance.
Recombinant LHPP protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), enables functional and mechanistic studies. Its production typically involves affinity tag-based purification (e.g., His-tag) to ensure high purity and activity. Recombinant LHPP is widely used to investigate enzymatic kinetics, substrate specificity, and interactions with potential inhibitors or therapeutic molecules. Additionally, it serves as a tool for developing diagnostic assays or exploring therapeutic strategies aimed at restoring LHPP activity in cancer cells.
Despite its significance, challenges remain in studying LHPP, such as understanding its full substrate spectrum and structural regulation. Further research is essential to unravel its precise pathophysiological roles and therapeutic potential.
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