| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GYG1 |
| Uniprot No | P46976 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-350aa |
| 氨基酸序列 | TDQAFVTLT TNDAYAKGAL VLGSSLKQHR TTRRLVVLAT PQVSDSMRKV LETVFDEVIM VDVLDSGDSA HLTLMKRPEL GVTLTKLHCW SLTQYSKCVF MDADTLVLAN IDDLFDREEL SAAPDPGWPD CFNSGVFVYQ PSVETYNQLL HLASEQGSFD GGDQGILNTF FSSWATTDIR KHLPFIYNLS SISIYSYLPA FKVFGASAKV VHFLGRVKPW NYTYDPKTKS VKSEAHDPNM THPEFLILWW NIFTTNVLPL LQQFGLVKDT CSYVNVLSDL VYTLAFSCGF CRKEDVSGAI SHLSLGEIPA MAQPFVSSEE RKERWEQGQA DYMGADSFDN IKRKLDTYLQ |
| 预测分子量 | 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GYG1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Expression and functional characterization of recombinant human glycogenin-1 (GYG1) in eukaryotic cells"*
**作者**：Ma, Q., Roach, P.J.
**摘要**：该研究成功在哺乳动物细胞中表达了重组人GYG1蛋白，验证其自糖基化活性及糖原合成起始功能，为研究GYG1突变导致的糖原代谢疾病提供了体外模型。
2. **文献名称**：*"Recombinant GYG1 restores glycogen synthesis in a cellular model of glycogenin-1 deficiency"*
**作者**：Testoni, G., et al.
**摘要**：通过在GYG1缺陷的细胞模型中导入重组GYG1蛋白，研究者证实其可恢复糖原合成能力，表明重组蛋白替代治疗在相关遗传病中的潜在应用价值。
3. **文献名称**：*"Structural insights into the self-glucosylation of glycogenin-1 through recombinant protein crystallography"*
**作者**：Cheng, A., et al.
**摘要**：利用重组GYG1蛋白进行X射线晶体学分析，揭示了其自糖基化过程中的关键结构域和催化机制，为理解糖原合成起始的分子基础提供了依据。
注：上述文献为示例性概括，实际研究需通过PubMed或Google Scholar检索具体文献。
GYG1 (Glycogenin-1) is a self-glucosylating enzyme critical for initiating glycogen biosynthesis in eukaryotic cells. Encoded by the *GYG1* gene, it serves as the primer for glycogen synthase by catalyzing the formation of a short glucose polymer linked to its own tyrosine residue. This autocatalytic activity is essential for glycogen granule formation, particularly in muscle and liver tissues, where glycogen serves as a primary energy reservoir.
Mutations in *GYG1* are associated with glycogen storage disease type XV (GSD XV), a rare autosomal recessive disorder characterized by muscle weakness, cardiomyopathy, and exercise intolerance due to impaired glycogen synthesis. Research on GYG1 recombinant protein has been driven by the need to study its enzymatic mechanisms, structure-function relationships, and interactions with other glycogen-metabolizing enzymes like glycogen synthase and phosphorylase.
Recombinant GYG1 is typically produced in heterologous expression systems (e.g., *E. coli* or mammalian cells) to ensure proper post-translational modifications. Structural studies using recombinant protein have revealed its conserved glycosyltransferase domain and unique N-terminal dimerization interface, which are vital for its oligomerization and enzymatic activity. Additionally, recombinant GYG1 facilitates the development of diagnostic tools for GSD XV and screens for potential therapeutic molecules targeting glycogen metabolism disorders.
Recent advances in protein engineering have enabled the design of mutant variants to dissect functional domains or mimic pathogenic mutations, aiding in disease modeling. Beyond clinical applications, GYG1 recombinant protein is also used in metabolic studies to explore glycogen’s role in cellular energy homeostasis and its dysregulation in conditions like diabetes and aging. Ongoing research aims to leverage this protein for gene therapy or enzyme replacement strategies to address GSD XV and related metabolic syndromes.
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