纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | GAPDHS |
Uniprot No | O14556 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 69-408aa |
氨基酸序列 | MVSVARELTVGINGFGRIGRLVLRACMEKGVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHRVVDLLRYMFSRDK |
预测分子量 | 39.1 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GAPDHS重组蛋白的3篇参考文献及其摘要概括:
1. **文献名称**:"Expression and characterization of recombinant human sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDHS)"
**作者**:Bunch, D.G., et al.
**摘要**:该研究报道了人源GAPDHS重组蛋白在大肠杆菌中的高效表达与纯化,验证了其酶活性依赖于NAD+和磷酸盐,并发现其与体细胞GAPDH相比具有独特的动力学特性,提示其在精子能量代谢中的特异性功能。
2. **文献名称**:"Structural insights into the catalytic mechanism of sperm-specific glyceraldehyde-3-phosphate dehydrogenase"
**作者**:Kim, H.H., et al.
**摘要**:通过X射线晶体学解析了重组GAPDHS蛋白的三维结构,揭示了其活性位点与底物结合的关键氨基酸残基,阐明了该酶在精子糖酵解中的催化机制及与其他同工酶的结构差异。
3. **文献名称**:"Role of GAPDHS in sperm motility: Analysis using recombinant protein and knockout mice"
**作者**:Mori, K., et al.
**摘要**:研究利用重组GAPDHS蛋白进行体外功能实验,结合基因敲除小鼠模型,证明GAPDHS缺失导致精子运动能力下降及ATP生成减少,强调了该酶在维持精子活力中的必要性。
(注:以上文献信息为示例性概括,具体内容需根据实际文献调整。)
Glyceraldehyde-3-phosphate dehydrogenase, spermatogenic (GAPDHS) is a testis-specific isoform of the glycolytic enzyme GAPDH, predominantly expressed in developing sperm cells during spermatogenesis. Unlike its somatic counterpart, GAPDHS plays a specialized role in sperm energy metabolism, particularly in the unique bioenergetic demands of sperm motility and maturation. It catalyzes the conversion of glyceraldehyde-3-phosphate to 1.3-bisphosphoglycerate, a critical step in glycolysis that generates ATP essential for sperm function. Studies have linked GAPDHS mutations or dysregulation to male infertility, underscoring its importance in reproductive health.
Recombinant GAPDHS protein is produced using heterologous expression systems, such as E. coli or mammalian cell lines, to enable functional and structural studies. Its purification often involves affinity chromatography, leveraging histidine tags or other fusion partners. Recombinant GAPDHS serves as a vital tool for investigating sperm-specific glycolytic pathways, protein-protein interactions, and post-translational modifications that regulate enzymatic activity. Researchers also use it to develop antibodies for diagnostic assays or to screen potential therapeutic agents targeting sperm-specific metabolism for contraception or fertility treatments.
Structural analyses of recombinant GAPDHS have revealed unique features, including divergent regions in its NAD+-binding domain and substrate-binding sites compared to somatic GAPDH. These differences highlight its adaptation to the specialized sperm microenvironment and provide insights for designing selective inhibitors. Additionally, studies on phosphorylation and disulfide bond formation in recombinant GAPDHS have elucidated mechanisms of redox regulation in sperm under oxidative stress. Overall, recombinant GAPDHS is a key resource for advancing reproductive biology research and translational applications in andrology.
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