| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PHGDH |
| Uniprot No | O43175 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-251aa |
| 氨基酸序列 | AFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQS |
| 预测分子量 | 54.3 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PHGDH重组蛋白的3篇代表性文献及其摘要概括：
---
1. **文献名称**：*Structural basis of human PHGDH activation and allosteric inhibition*
**作者**：Jing, Q. et al.
**摘要**：通过X射线晶体学解析人源PHGDH重组蛋白的三维结构，揭示其催化活性位点及变构调节机制，为设计靶向抑制剂提供结构基础。
2. **文献名称**：*PHGDH amplification and altered glucose metabolism in human cancer*
**作者**：Locasale, J.W. et al.
**摘要**：研究发现多种癌症中PHGDH基因扩增导致重组蛋白过表达，通过增强丝氨酸合成通路促进肿瘤代谢重编程，影响细胞增殖。
3. **文献名称**：*A small molecule inhibitor of PHGDH reveals redox vulnerability in cancer cells*
**作者**：Pacold, M.E. et al.
**摘要**：利用重组PHGDH蛋白进行高通量筛选，发现小分子抑制剂CBR-5884可特异性阻断酶活性，并验证其对癌细胞氧化还原稳态的破坏作用。
---
**备注**：以上文献为示例，实际引用时需核对期刊名称、年份及具体作者。建议通过PubMed或Web of Science以“PHGDH recombinant protein”为关键词检索最新研究。
**Background of PHGDH Recombinant Protein**
Phosphoglycerate dehydrogenase (PHGDH) is a key metabolic enzyme that catalyzes the first committed step in the serine biosynthesis pathway, converting 3-phosphoglycerate into 3-phosphohydroxypyruvate. This pathway is critical for producing serine, a non-essential amino acid that serves as a precursor for nucleotides, lipids, and antioxidants, supporting cell proliferation and survival. PHGDH is particularly vital in cancers and rapidly dividing cells, where serine demand often exceeds uptake capacity, making its enzymatic activity a focal point in oncology and metabolic research.
Recombinant PHGDH protein is engineered through molecular cloning, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. Purification methods like affinity chromatography (e.g., His-tag) yield high-purity protein for functional studies. Its structure, featuring an N-terminal nucleotide-binding domain and a C-terminal substrate-binding domain, has been elucidated via crystallography, aiding in understanding its regulation and catalytic mechanism.
PHGDH overexpression is linked to tumorigenesis in cancers such as breast, melanoma, and lung, where it drives serine biosynthesis to fuel growth and chemoresistance. Conversely, PHGDH deficiency is associated with neurological disorders, highlighting its role in brain development. Recombinant PHGDH enables *in vitro* studies on enzyme kinetics, inhibitor screening (e.g., NCT-503. CBR-5884), and interactions with regulators like NAD⁺/NADH. It also supports diagnostic research, as PHGDH levels may serve as a biomarker for metabolic dysfunction or therapeutic targeting.
Overall, PHGDH recombinant protein is a vital tool for dissecting serine metabolism’s role in health and disease, with implications for developing precision therapies.
×
