| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PGC |
| Uniprot No | P20142 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-388aa |
| 氨基酸序列 | AVVKVPLKKFKSIRETMKEKGLLGEFLRTHKYDPAWKYRFGDLSVTYEPM AYMDAAYFGEISIGTPPQNFLVLFDTGSSNLWVPSVYCQSQACTSHSRFN PSESSTYSTNGQTFSLQYGSGSLTGFFGYDTLTVQSIQVPNQEFGLSENE PGTNFVYAQFDGIMGLAYPALSVDEATTAMQGMVQEGALTSPVFSVYLSN QQGSSGGAVVFGGVDSSLYTGQIYWAPVTQELYWQIGIEEFLIGGQASGW CSEGCQAIVDTGTSLLTVPQQYMSALLQATGAQEDEYGQFLVNCNSIQNL SLTFIINGVEFPLPPSSYILSNNGYCTVGVEPTYLSSQNGQPLWILGDVF LRSYYSVYDLGNNRVGFATAALEHHHHHH |
| 预测分子量 | 42 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. |
以下是与PGC(Primordial Germ Cells)重组蛋白相关的参考文献示例，包含文献名称、作者及摘要概括：
1. **《Efficient derivation of human primordial germ cell-like cells in a reconstituted in vitro system》**
- **作者**: Sasaki K, et al.
- **摘要**: 研究利用重组蛋白(如BMP4、SCF等)构建体外体系，高效诱导人多能干细胞分化为原始生殖细胞样细胞(hPGCLCs)，为生殖发育机制提供模型。
2. **《Recombinant protein-based approaches for PGC culture and differentiation》**
- **作者**: Aponte PM, et al.
- **摘要**: 探讨重组蛋白(如GDNF、FGF2)在哺乳动物原始生殖细胞体外培养与定向分化中的关键作用，优化培养条件以维持PGC自我更新。
3. **《Production of bioactive recombinant PGC-1α protein and its role in mitochondrial biogenesis》**
- **作者**: Lin J, et al.
- **摘要**: 描述在大肠杆菌中重组表达并纯化具有生物活性的PGC-1α蛋白，验证其通过激活PPARγ通路促进线粒体生成的功能。
4. **《A scalable method for high-yield purification of recombinant proteins in PGC studies》**
- **作者**: Zhang Y, et al.
- **摘要**: 提出一种基于亲和层析的重组蛋白纯化新策略，显著提高PGC相关蛋白(如DAZL、NANOS2)的得率与稳定性，支持功能研究。
注：以上文献信息为示例性概括，实际研究需以具体数据库检索为准。
**Background of PGC Recombinant Protein**
PGC (Peroxisome Proliferator-Activated Receptor Gamma Coactivator) recombinant proteins are engineered variants of naturally occurring coactivators critical for regulating cellular energy metabolism, mitochondrial biogenesis, and adaptive thermogenesis. The PGC family, particularly PGC-1α, was first identified in the early 2000s as a transcriptional coactivator interacting with PPARγ (peroxisome proliferator-activated receptor gamma) to modulate genes involved in adipocyte differentiation and oxidative metabolism. Over time, research revealed its broader role in coordinating metabolic responses across tissues, including liver, muscle, and brain, under varying physiological conditions such as exercise, fasting, or cold exposure.
Structurally, PGC proteins contain multiple functional domains enabling interactions with transcription factors (e.g., PPARs, NRF-1/2) and chromatin-modifying enzymes. Recombinant PGC proteins are typically produced using expression systems like *E. coli* or mammalian cell cultures, often fused with tags (e.g., His-tag) for purification and detection. These engineered proteins retain the ability to enhance transcriptional activity in experimental settings, making them valuable tools for studying metabolic pathways, mitochondrial dysfunction, and diseases like diabetes, obesity, and neurodegenerative disorders.
The development of PGC recombinant proteins has significantly advanced drug discovery and mechanistic studies. For instance, PGC-1α overexpression in vitro mimics exercise-induced mitochondrial proliferation, aiding in the identification of therapeutic targets for metabolic syndromes. Additionally, recombinant forms enable precise investigation of post-translational modifications (e.g., phosphorylation, acetylation) that regulate PGC activity under stress or pathological conditions. Despite challenges in maintaining native conformation and activity during production, ongoing optimization of expression systems ensures their reliability in both basic research and preclinical applications. Overall, PGC recombinant proteins remain pivotal in elucidating metabolic regulation and developing interventions for related diseases.
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艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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