| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PGK1 |
| Uniprot No | P00558 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-417aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSLSNKLTLDKLDVKGKRVVMRVDFNVPMK NNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEP VAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEG KGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVN LPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDK VNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKI TLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPESSKKYAEAVTR AKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCC AKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI |
| 预测分子量 | 47 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PGK1重组蛋白的参考文献示例(仅供参考，具体文献需通过学术数据库验证)：
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1. **文献名称**：*"High-level expression and purification of recombinant human phosphoglycerate kinase 1 (PGK1) in Escherichia coli"*
**作者**：Zhang Y, et al.
**摘要**：本研究报道了一种在大肠杆菌中高效表达和纯化重组人PGK1的方法，通过优化表达条件和层析技术获得高纯度蛋白，并证实其具有与天然PGK1相似的酶活性，为功能研究奠定基础。
2. **文献名称**：*"Crystal structure of recombinant Plasmodium falciparum PGK1: Insights into antimalarial drug design"*
**作者**：Shah S, et al.
**摘要**：解析了恶性疟原虫重组PGK1的晶体结构，揭示了其底物结合位点和构象变化，为基于PGK1结构的抗疟药物开发提供了理论依据。
3. **文献名称**：*"Recombinant PGK1 promotes tumor angiogenesis through extracellular vesicle-mediated signaling"*
**作者**：Wang L, et al.
**摘要**：研究发现重组PGK1可通过外泌体途径激活内皮细胞，促进肿瘤血管生成，提示PGK1在肿瘤微环境中的非经典功能。
4. **文献名称**：*"Functional analysis of recombinant PGK1 mutations linked to neurodegenerative disorders"*
**作者**：Chen R, et al.
**摘要**：通过体外表达携带神经退行性疾病相关突变的PGK1重组蛋白，发现其酶活性和稳定性显著降低，揭示了突变导致代谢功能障碍的分子机制。
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**注意**：以上文献信息为示例，实际引用时请通过PubMed、Google Scholar等平台检索真实文献。
Phosphoglycerate kinase 1 (PGK1) is a ubiquitously expressed metabolic enzyme encoded by the PGK1 gene located on the X chromosome. As a key component of glycolysis, it catalyzes the ATP-generating step by transferring a phosphate group from 1.3-bisphosphoglycerate to ADP, yielding 3-phosphoglycerate and ATP. Beyond its canonical role in energy metabolism, PGK1 has emerged as a multifunctional protein involved in diverse cellular processes, including autophagy, DNA repair, and cell migration. Its dysregulation is implicated in pathological conditions such as cancer, neurodegenerative disorders, and infectious diseases.
Recombinant PGK1 protein is produced using genetic engineering techniques, typically through expression in bacterial (e.g., E. coli) or eukaryotic systems, followed by purification via affinity chromatography. This engineered protein retains the enzymatic activity and structural features of native PGK1. including its two distinct domains that undergo conformational changes during substrate binding. The recombinant form enables precise study of PGK1's molecular mechanisms without interference from cellular components.
Research applications span both basic and translational science. In cancer biology, PGK1 overexpression has been linked to tumor progression through dual roles in regulating metabolic reprogramming and acting as a protein kinase to activate oncogenic pathways. In neurodegenerative contexts, abnormal PGK1 function correlates with amyloid-beta aggregation in Alzheimer's disease. Additionally, recombinant PGK1 serves as a potential therapeutic target, with inhibitors being explored for anticancer strategies and activators investigated for metabolic disorders. Its autocrine signaling function in angiogenesis further highlights therapeutic relevance for ischemic conditions. The development of recombinant variants with modified enzymatic properties continues to expand its utility in dissecting metabolic flexibility in disease models.
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