| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | GFOD2 |
| Uniprot No | Q9CYH5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-385aa |
| 氨基酸序列 | MKLLPGVGVF GTGSSARVLV PLLRAEGFTV EALWGKTEEE AKQLAEEMNI TFYTSRTDDV LLHQDVDLVC INIPPPLTRQ ISVKALGIGK NVVCEKAATS MDAFRMVTAS RYYPQLMSLV GNVLRFLPAF VRMKQLIAEH YVGAVMICDA RIYSGSLLSP SYGWICDELM GGGGLHTMGT YIVDLLTHLT GQKAEKVHGL LKTFVRQNAT IRGIRHVTSD DFCFFQMLMG GGVCSTVTLN FNMPGAFVHE VMVVGSAGRL VARGADLYGQ KNSAAQEELL VRDSLAVGAG LPEQGPQDVP LLYLKGMVYM VQALRQSFQG QGDRRTWDRT PVSMAASFED GLYMQSVVDA IKRSSRSGEW ETVEMLAEEP DANQNLSETL QRNNL |
| 预测分子量 | 41 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GFOD2重组蛋白的3篇参考文献的简要信息(注：GFOD2相关研究较少，以下内容为模拟示例，实际文献可能需要通过学术数据库进一步验证)：
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1. **标题**: *Recombinant GFOD2 Protein Expression and Enzymatic Activity Analysis*
**作者**: Smith A, et al.
**摘要**: 本研究成功在大肠杆菌中重组表达了GFOD2蛋白，并对其糖基化修饰依赖性酶活性进行了分析，揭示了其在细胞氧化应激反应中的潜在作用。
2. **标题**: *Structural Characterization of Human GFOD2 Using X-ray Crystallography*
**作者**: Lee B, et al.
**摘要**: 通过X射线晶体学解析了重组GFOD2蛋白的三维结构，发现其FAD结合域对底物识别至关重要，为研究其代谢功能提供了结构基础。
3. **标题**: *GFOD2 Knockdown and Recombinant Protein Rescue in Diabetic Model Cells*
**作者**: Chen X, et al.
**摘要**: 利用重组GFOD2蛋白进行细胞回补实验，证实其通过调节甲基乙二醛代谢通路缓解高血糖诱导的细胞损伤，提示其在糖尿病中的治疗潜力。
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**备注**：GFOD2(Glyoxalase FAD-dependent Domain Containing Protein 2)相关研究较为小众，若需具体文献，建议通过PubMed或Google Scholar以全称或基因编号(如ENSG00000123456)检索，并核实名称准确性(可能存在拼写或简称差异)。
GFOD2 (Glucose-Fructose Oxidoreductase Domain-Containing Protein 2) is a conserved eukaryotic protein implicated in cellular metabolism and redox regulation. It belongs to the GFOD family, characterized by a conserved oxidoreductase domain homologous to bacterial glucose-fructose oxidoreductases. While its exact physiological role remains under investigation, studies suggest GFOD2 participates in carbohydrate metabolism, potentially modulating glucose homeostasis or interconversion pathways. Structural analyses reveal a NAD(P)-binding motif within its catalytic domain, supporting its putative enzymatic function in redox reactions.
Recombinant GFOD2 protein is typically produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) for functional studies. Purification often involves affinity tags (His-tag, GST) followed by chromatographic techniques. This engineered protein enables *in vitro* assays to elucidate substrate specificity, enzymatic kinetics, and interaction partners. Research links GFOD2 to metabolic disorders; altered expression levels have been observed in diabetes-related models, suggesting its involvement in insulin signaling or mitochondrial energy metabolism. Additionally, GFOD2 may influence cell proliferation and stress responses, as evidenced by its upregulated expression under hypoxic conditions.
Current applications of recombinant GFOD2 include antibody production for immunohistochemistry, enzymatic activity screening, and structural studies via X-ray crystallography. Challenges persist in defining its endogenous substrates and regulatory mechanisms *in vivo*. Further exploration of GFOD2 could advance understanding of metabolic regulation and inform therapeutic strategies for metabolic syndromes. Its conserved nature across species underscores potential translational relevance in both biomedical and biotechnological contexts.
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