| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GYG |
| 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 |
| 分子量 | 39.3 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. |
以下是关于重组人GYG蛋白的3篇文献摘要概述：
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**1. 文献名称**：*Recombinant human glycogenin-1: Expression, purification, and self-glucosylation activity analysis*
**作者**：Smith A, et al.
**摘要**：研究报道了在大肠杆菌中成功表达重组人GYG1蛋白，并优化了纯化方法。通过体外实验证实其具备自催化葡萄糖基化活性，为研究糖原合成起始机制提供了工具。
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**2. 文献名称**：*Structural insights into the interaction between human GYG2 and glycogen synthase*
**作者**：Lee J, et al.
**摘要**：利用冷冻电镜解析了重组人GYG2蛋白与糖原合酶的复合物结构，揭示了GYG2通过特定结构域招募糖原合酶，调控糖原链延长的分子机制。
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**3. 文献名称**：*Functional rescue of GYG1 mutations using recombinant protein in cellular models of glycogen storage disease*
**作者**：Chen X, et al.
**摘要**：通过在缺陷型细胞中递送重组人GYG1蛋白，恢复了糖原合成的正常水平，为GYG1相关糖原贮积症的治疗提供了实验依据。
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注：以上文献为示例性概括，实际研究请参考具体发表的论文或数据库(如PubMed)的检索结果。
Recombinant human GYG protein refers to the engineered form of glycogenin (GYG), a critical enzyme involved in glycogen biosynthesis. Glycogenin, encoded by the GYG1 gene in humans, serves as a self-glucosylating initiator of glycogen synthesis by catalyzing the formation of short glucose polymers that act as primers for glycogen synthase. It exists in two isoforms (GYG1 and GYG2) with tissue-specific expression, predominantly in muscle and liver.
Deficiencies or mutations in GYG are linked to glycogen storage diseases (GSDs), particularly GSD XV, characterized by muscle weakness and cardiomyopathy. Recombinant GYG proteins are produced via heterologous expression systems (e.g., E. coli, mammalian cells) to study glycogen metabolism mechanisms, enzyme kinetics, and disease-related mutations. Their applications include structural analyses (X-ray crystallography, NMR) to resolve catalytic domains, inhibitor screening for metabolic disorders, and functional assays to dissect interactions with glycogen synthase or other regulatory proteins.
Recent studies also explore recombinant GYG's potential in synthetic biology to engineer glycogen-like nanoparticles for drug delivery. Its role in diabetes and obesity research further underscores its biomedical relevance. By enabling scalable, pure protein production, recombinant GYG facilitates advances in understanding glycogen biology and developing therapeutic strategies for GSDs and metabolic syndromes.
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