| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PYGB |
| Uniprot No | P11216 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 477-731aa |
| 氨基酸序列 | PEKF QNKTNGITPR RWLLLCNPGL ADTIVEKIGE EFLTDLSQLK KLLPLVSDEV FIRDVAKVKQ ENKLKFSAFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKRDPAKAFV PRTVMIGGKA APGYHMAKLI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR VSLAEKVIPA ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGAENLF IFGLRVEDVE ALDRKGYNAR E |
| 预测分子量 | 32 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PYGB(糖原磷酸化酶脑型同工酶)重组蛋白的模拟参考文献示例，供参考：
1. **文献名称**：*"Expression and purification of recombinant human PYGB in Escherichia coli: Enzymatic characterization and role in glycogen metabolism"*
**作者**：Smith J et al. (2015)
**摘要**：研究报道了在大肠杆菌中高效表达并纯化人源PYGB重组蛋白的过程，验证其磷酸化酶活性，并探讨其在糖原分解代谢中的调控机制。
2. **文献名称**：*"PYGB promotes tumor progression via enhancing glycogenolysis in triple-negative breast cancer"*
**作者**：Zhang L et al. (2018)
**摘要**：通过重组PYGB蛋白的功能实验，揭示了其在三阴性乳腺癌中通过加速糖原分解为癌细胞提供能量，促进肿瘤增殖和转移的分子机制。
3. **文献名称**：*"Structural insights into the allosteric regulation of PYGB by phosphorylation"*
**作者**：Chen X et al. (2020)
**摘要**：利用重组PYGB蛋白结合X射线晶体学技术，解析了其磷酸化修饰后的构象变化，阐明了磷酸化如何调控PYGB与其他代谢酶的相互作用。
4. **文献名称**：*"Recombinant PYGB as a potential therapeutic target in neurodegenerative diseases"*
**作者**：Brown K et al. (2022)
**摘要**：研究基于重组PYGB蛋白的体外模型，发现抑制其活性可减少神经细胞中异常糖原积累，为阿尔茨海默病等疾病提供了潜在治疗策略。
**注意**：以上文献为模拟内容，实际研究需通过PubMed、Web of Science等平台检索真实文献。
**Background of PYGB Recombinant Protein**
PYGB (glycogen phosphorylase, brain-type) is a critical enzyme in glycogen metabolism, primarily expressed in the brain and other tissues. It catalyzes the rate-limiting step of glycogenolysis, breaking down glycogen into glucose-1-phosphate to maintain cellular energy homeostasis, particularly under conditions of metabolic stress. As an isoform of glycogen phosphorylase, PYGB differs from its liver (PYGL) and muscle (PYGM) counterparts in regulatory mechanisms and tissue-specific functions, reflecting adaptations to the brain’s unique energy demands.
Structurally, PYGB is a homodimer regulated by allosteric effectors (e.g., AMP, ATP) and reversible phosphorylation. Its activity is tightly linked to cellular energy status, making it a key player in balancing glucose availability during hypoxia, ischemia, or neuronal activation. Dysregulation of PYGB has been implicated in neurodegenerative diseases, such as Alzheimer’s disease, and metabolic disorders, where impaired glycogen turnover contributes to pathology.
Recombinant PYGB protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to study its biochemical properties, structure-function relationships, and interactions with modulators. Purification techniques, such as affinity chromatography, ensure high purity and activity. This recombinant tool enables research into glycogen metabolism in neurological contexts, drug screening for metabolic disorders, and exploration of PYGB’s role in cancer, where aberrant glycogen utilization supports tumor survival.
Additionally, PYGB recombinant protein serves as a potential therapeutic target or diagnostic biomarker, particularly in conditions linked to energy dysregulation. Its study advances understanding of brain energetics and offers insights into novel treatments for metabolic and neurodegenerative diseases.
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