纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PGM3 |
Uniprot No | O95394 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-542aa |
氨基酸序列 | MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQDMQRVLIDISEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELLVEIGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKQSAEQLEDKKRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIGERPQPGF |
预测分子量 | 75.9kDa |
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PGM3重组蛋白的3篇参考文献示例(注:以下内容为示例性概括,具体文献需通过学术数据库检索确认):
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1. **文献名称**:*Expression and characterization of recombinant human phosphoglucomutase 3 (PGM3) in Escherichia coli*
**作者**:Smith A, et al.
**摘要**:该研究报道了人源PGM3基因在大肠杆菌中的重组表达及纯化,分析了重组蛋白的酶活性,并验证其与先天性糖基化缺陷疾病的相关性。
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2. **文献名称**:*Structural insights into PGM3 deficiency-associated disorders through recombinant protein crystallography*
**作者**:Chen L, et al.
**摘要**:通过重组表达PGM3蛋白并进行X射线晶体学分析,揭示了PGM3突变导致酶功能异常的分子机制,为相关免疫疾病的治疗提供结构基础。
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3. **文献名称**:*Functional analysis of recombinant PGM3 variants in glycosylation pathways*
**作者**:Wang Y, et al.
**摘要**:研究利用昆虫细胞系统表达多种PGM3突变体重组蛋白,发现特定突变体导致糖基化通路异常,阐明了PGM3在代谢中的关键作用。
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**提示**:建议通过PubMed、Google Scholar等平台,以关键词“recombinant PGM3 protein”“PGM3 expression”检索最新文献,或查阅《Journal of Biological Chemistry》《Biochemical Journal》等期刊相关主题论文。
**Background of PGM3 Recombinant Protein**
Phosphoglucomutase 3 (PGM3) is a key enzyme in carbohydrate metabolism, catalyzing the interconversion of glucose-1-phosphate and glucose-6-phosphate. This reversible reaction is critical for glycogen synthesis, glycolysis, and nucleotide sugar production, which supports glycosylation processes essential for protein and lipid function. PGM3 belongs to the phosphoglucomutase family and is highly expressed in tissues requiring dynamic glucose metabolism, such as the liver, muscle, and immune cells.
PGM3 gained significant attention due to its association with genetic disorders. Biallelic mutations in the *PGM3* gene are linked to a rare autosomal recessive immunodeficiency syndrome characterized by impaired glycosylation of proteins (CDG, congenital disorder of glycosylation). This condition manifests as recurrent infections, autoimmune dysregulation, and developmental delays, underscoring PGM3's role in immune cell function and systemic homeostasis.
Recombinant PGM3 protein is produced using biotechnological platforms (e.g., bacterial or mammalian expression systems) to generate purified, active enzyme for research and therapeutic development. Its recombinant form retains the enzymatic activity and structural features of the native protein, enabling studies on substrate specificity, kinetic properties, and interaction with regulatory molecules. Researchers utilize recombinant PGM3 to investigate glycosylation defects, screen potential enzyme modulators, and explore gene therapy strategies for PGM3-deficient conditions.
Recent studies also highlight PGM3's involvement in cancer metabolism and immune evasion, where altered glycosylation patterns influence tumor progression. The recombinant protein serves as a tool to dissect these mechanisms, offering insights into targeted therapies. Overall, PGM3 recombinant protein bridges fundamental biochemistry with translational applications, addressing both metabolic disorders and broader disease contexts.
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