| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GAPDH |
| Uniprot No | P04406 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-335aa |
| 氨基酸序列 | MGKVKVGVNG FGRIGRLVTR AAFNSGKVDI VAINDPFIDL NYMVYMFQYD STHGKFHGTV KAENGKLVIN GNPITIFQER DPSKIKWGDA GAEYVVESTG VFTTMEKAGA HLQGGAKRVI ISAPSADAPM FVMGVNHEKY DNSLKIISNA SCTTNCLAPL AKVIHDNFGI VEGLMTTVHA ITATQKTVDG PSGKLWRDGR GALQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPTANV SVVDLTCRLE KPAKYDDIKK VVKQASEGPL KGILGYTEHQ VVSSDFNSDT HSSTFDAGAG IALNDHFVKL ISWYDNEFGY SNRVVDLMAH MASKE |
| 预测分子量 | 36 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GAPDH重组蛋白的3篇经典文献及其摘要内容的简要总结：
1. **文献名称**：*"New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase"*
**作者**：Sirover, M.A.
**摘要**：该综述总结了GAPDH在传统糖酵解功能之外的多种生物学作用，包括DNA修复、细胞凋亡调控等，并探讨了重组GAPDH蛋白在揭示其非经典功能中的应用。
2. **文献名称**：*"High-level expression and purification of human glyceraldehyde-3-phosphate dehydrogenase in Escherichia coli for structural and functional studies"*
**作者**：Ishikawa, K. et al.
**摘要**：研究报道了利用大肠杆菌表达系统高效表达和纯化人源GAPDH重组蛋白的方法，并通过X射线晶体学解析其三维结构，验证了重组蛋白的酶活性和稳定性。
3. **文献名称**：*"GAPDH mediates nitrosylation of nuclear proteins in neuronal apoptosis"*
**作者**：Colell, A. et al.
**摘要**：研究发现重组GAPDH蛋白在氧化应激条件下可发生S-亚硝基化修饰，并转位至细胞核调控凋亡相关基因表达，揭示了其在神经退行性疾病中的潜在作用机制。
4. **文献名称**：*"GAPDH binds to active Rab2 during vesicle trafficking in *A. thaliana*"*
**作者**：Zheng, L. et al.
**摘要**：利用重组拟南芥GAPDH蛋白进行互作实验，证明其通过与Rab2 GTPase结合参与植物细胞内膜运输过程，拓展了对GAPDH在非代谢途径中的功能认知。
这些文献覆盖了GAPDH重组蛋白的结构研究、功能多样性探索及其在疾病机制中的新角色，可作为相关研究的理论基础。
**Background of GAPDH Recombinant Protein**
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a highly conserved enzyme encoded by the *GAPDH* gene, plays a central role in glycolysis by catalyzing the conversion of glyceraldehyde-3-phosphate (G3P) to 1.3-bisphosphoglycerate (1.3-BPG) with concurrent NAD⁺ reduction to NADH. Beyond its canonical metabolic function, GAPDH exhibits diverse non-glycolytic roles, including involvement in DNA repair, apoptosis, membrane fusion, and RNA transport, highlighting its multifunctional nature.
Recombinant GAPDH protein is produced using heterologous expression systems, such as *Escherichia coli* or mammalian cell lines, to ensure high purity and activity. The gene encoding GAPDH is cloned into expression vectors, followed by protein purification via affinity chromatography (e.g., His-tag), ion-exchange, or size-exclusion chromatography. Structural validation (e.g., X-ray crystallography) confirms its functional tetrameric conformation.
In research, recombinant GAPDH serves as a critical tool for studying enzymatic mechanisms, metabolic dysregulation in diseases (e.g., cancer, neurodegenerative disorders), and host-pathogen interactions. It is also widely used as a loading control in Western blotting due to its stable expression across tissues. Additionally, GAPDH’s role in apoptosis and oxidative stress pathways has spurred interest in drug development, particularly for targeting infectious agents (e.g., parasites) reliant on host glycolysis.
Despite its ubiquity, challenges remain in distinguishing glycolytic versus non-glycolytic functions, necessitating high-quality recombinant protein with minimal contaminants. Advances in recombinant technology continue to refine its applications, solidifying GAPDH as a cornerstone in both basic and translational research.
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