| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PHKG1 |
| Uniprot No | Q16816 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-387 aa |
| 活性数据 | TRDEALPDS HSAQDFYENY EPKEILGRGV SSVVRRCIHK PTSQEYAVKV IDVTGGGSFS PEEVRELREA TLKEVDILRK VSGHPNIIQL KDTYETNTFF FLVFDLMKRG ELFDYLTEKV TLSEKETRKI MRALLEVICT LHKLNIVHRD LKPENILLDD NMNIKLTDFG FSCQLEPGER LREVCGTPSY LAPEIIECSM NEDHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR MIMSGNYQFG SPEWDDYSDT VKDLVSRFLV VQPQNRYTAE EALAHPFFQQ YLVEEVRHFS PRGKFKVIAL TVLASVRIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY AFRIYGHWVK KGQQQNRAAL FENTPKAVLL SLAEEDY |
| 分子量 | 45.0 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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3篇关于重组人PHKG1蛋白的研究文献示例：
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1. **标题**：Structural and Functional Analysis of Human Phosphorylase Kinase Subunit PHKG1
**作者**：Li X, et al.
**摘要**：本研究通过大肠杆菌表达系统成功获得重组人PHKG1蛋白，解析其晶体结构为2.1Å分辨率，揭示了其磷酸化酶激酶活性调控的关键结构域，并验证其与肝糖原代谢相关的生物学功能。
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2. **标题**：Recombinant PHKG1 Expression and Its Role in Hepatocellular Carcinoma
**作者**：Wang Y, et al.
**摘要**：利用哺乳动物细胞系统表达重组PHKG1.发现其异常表达通过激活糖原磷酸化酶通路促进肝癌细胞增殖，提示PHKG1可能作为肝癌治疗靶点。
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3. **标题**：Functional Characterization of PHKG1 Mutations in Glycogen Storage Disease
**作者**：Zhang R, et al.
**摘要**：构建重组突变体PHKG1蛋白，证明某些遗传突变导致激酶活性丧失，与IX型糖原贮积症的发病机制直接相关，为疾病诊断提供分子依据。
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**备注**：以上文献信息为模拟示例，实际文献需通过PubMed或Web of Science检索(关键词：PHKG1 recombinant、phosphorylase kinase gamma 1)。建议结合具体研究方向筛选近年高质量论文。
Phosphorylase kinase γ1 (PHKG1) is a catalytic subunit of the phosphorylase kinase (PhK) complex, which plays a critical role in glycogen metabolism. As part of the PhK holoenzyme, PHKG1 regulates the activation of glycogen phosphorylase, an enzyme essential for glycogen breakdown to release glucose-1-phosphate during energy demand. Structurally, PHKG1 belongs to the calcium/calmodulin-dependent protein kinase family and requires calcium ions for its activity. It is predominantly expressed in the liver and skeletal muscle, where glycogen storage and mobilization are tightly regulated.
Recombinant human PHKG1 protein is produced through molecular cloning and expression in heterologous systems (e.g., E. coli or mammalian cells), enabling controlled in vitro studies. This approach allows researchers to explore PHKG1’s enzymatic properties, interaction networks, and regulatory mechanisms without interference from other PhK subunits. PHKG1 dysfunction has been linked to metabolic disorders, including glycogen storage disease type 9D (GSD9D), characterized by hepatomegaly and hypoglycemia. Studies using recombinant PHKG1 also contribute to understanding its phosphorylation dynamics, calcium/calmodulin dependency, and potential cross-talk with other signaling pathways involved in energy homeostasis. Additionally, the recombinant protein serves as a tool for drug screening targeting glycogen-related metabolic diseases.
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