| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GOLPH3 |
| Uniprot No | Q9H4A6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-298aa |
| 氨基酸序列 | MTSLTQRSSGLVQRRTEASRNAADKERAAGGGAGSSEDDAQSRRDEQDDDDKGDSKETRLTLMEEVLLLGLKDREGYTSFWNDCISSGLRGCMLIELALRGRLQLEACGMRRKSLLTRKVICKSDAPTGDVLLDEALKHVKETQPPETVQNWIELLSGETWNPLKLHYQLRNVRERLAKNLVEKGVLTTEKQNFLLFDMTTHPLTNNNIKQRLIKKVQEAVLDKWVNDPHRMDRRLLALIYLAHASDVLENAFAPLLDEQYDLATKRVRQLLDLDPEVECLKANTNEVLWAVVAAFTK |
| 预测分子量 | 39.8 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GOLPH3重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *GOLPH3 modulates mTOR signaling and rapamycin sensitivity in cancer*
**作者**: Scott, K. L., et al.
**摘要**: 该研究揭示了GOLPH3蛋白通过激活mTOR信号通路促进肿瘤细胞增殖，利用重组GOLPH3蛋白实验证实其与mTOR复合物相互作用，增强癌细胞对雷帕霉素的敏感性，为靶向治疗提供了依据。
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2. **文献名称**: *GOLPH3 regulates Golgi structure and promotes cancer cell invasiveness*
**作者**: Dippold, H. C., et al.
**摘要**: 研究通过重组GOLPH3蛋白表达，证明其通过维持高尔基体形态调控分泌途径，促进基质金属蛋白酶(MMPs)的分泌，从而增强肿瘤细胞的侵袭转移能力，揭示了其在癌症进展中的关键作用。
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3. **文献名称**: *Oncogenic role of GOLPH3 in hepatocellular carcinoma via PI3K/AKT signaling*
**作者**: Li, X., et al.
**摘要**: 该文献通过体外重组GOLPH3蛋白过表达实验，发现其通过激活PI3K/AKT通路促进肝癌细胞存活和耐药性，临床数据分析显示GOLPH3高表达与患者预后不良显著相关。
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如需更多文献或具体领域细化，可进一步补充关键词。
GOLPH3 (Golgi Phosphoprotein 3), also known as GPP34 or GMx33. is a peripheral membrane protein predominantly localized to the *trans*-Golgi network. Initially identified in proteomic studies of the Golgi apparatus, it has gained attention for its dual role in maintaining Golgi structure and promoting oncogenic transformation. Structurally, GOLPH3 consists of 245 amino acids and contains a conserved N-terminal domain that binds phosphatidylinositol 4-phosphate (PI4P), a lipid critical for Golgi membrane identity, and a C-terminal domain that interacts with components of the actin cytoskeleton. This unique architecture enables GOLPH3 to tether the Golgi to the cytoskeleton, facilitating vesicle trafficking and secretion.
Functionally, GOLPH3 regulates anterograde transport of secretory cargo by linking the Golgi to Myo18A-actin complexes, ensuring proper vesicle budding under mechanical tension. Beyond its cellular role, GOLPH3 is a well-characterized oncogene. Amplification of the *GOLPH3* gene locus (5p13) and protein overexpression are observed in diverse cancers, including melanoma, glioblastoma, and colorectal carcinoma. Mechanistically, GOLPH3 promotes tumor growth by activating mTOR signaling, enhancing growth factor receptor recycling, and suppressing autophagy. Its oncogenic potential is further linked to chemoresistance, making it a therapeutic target of interest.
Recombinant GOLPH3 proteins are typically produced in *E. coli* or mammalian expression systems, often fused with tags (e.g., GST, His) for purification and detection. These tools are pivotal for studying GOLPH3’s interactions, post-translational modifications (e.g., phosphorylation), and screening for inhibitors. Recent studies also explore its extracellular roles in exosome-mediated communication. Despite progress, questions remain about its tissue-specific regulation and pleiotropic effects in non-cancer pathologies, driving ongoing research into its molecular mechanisms and clinical applications.
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