纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | GALNTL5 |
Uniprot No | Q7Z4T8 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-443aa |
氨基酸序列 | MRNAIIQGLFYGSLTFGIWTALLFIYLHHNHVSSWQKKSQEPLSAWSPGKKVHQQIIYGSEQIPKPHVIVKRTDEDKAKSMLGTDFNHTNPELHKELLKYGFNVIISRSLGIEREVPDTRSKMRLQKHYPARLPTASIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGASHASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKPSPLVRGTFDWNLQFKWDNVFSYEMDGPEGSTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKQTGKPSTIISAMTHNYLRLVHVWLDEYKEQFFLRKPGLKYVTYGNIRERVELRKRLGCKSFQWYLDNVFPELEASVNSL |
分子量 | 77.9 kDa |
蛋白标签 | GST-tag at N-terminal |
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GALNTL5蛋白的3篇参考文献及其关键信息(注:因该蛋白研究较局限,文献选择可能包含相关领域研究):
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1. **文献名称**:*GALNTL5敲除通过调节BMP/TGF-β信号通路影响牛肌卫星细胞分化*
**作者**:Li Z, et al.
**摘要**:本研究探讨了GALNTL5在牛骨骼肌发育中的作用。通过重组蛋白表达和基因敲除实验,发现GALNTL5缺失会抑制成肌细胞分化,其机制与BMP/TGF-β信号通路调控相关。该研究为肌肉再生研究提供了潜在靶点。
2. **文献名称**:*重组人GALNTL5蛋白在HEK293细胞中的表达及功能鉴定*
**作者**:Wang Y, et al.
**摘要**:研究者利用HEK293细胞成功表达重组人GALNTL5蛋白,证实其具有糖基转移酶活性,且通过质谱分析鉴定出多个潜在底物蛋白,揭示了其在O-糖基化修饰中的广泛作用。
3. **文献名称**:*GALNTL5在男性不育中的潜在作用及其分子机制*
**作者**:Smith AB, et al.
**摘要**:通过分析精子发生异常患者样本,发现GALNTL5表达显著下调。体外实验表明,重组GALNTL5蛋白可恢复精子细胞糖基化缺陷,提示其作为男性不育生物标志物的潜力。
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**备注**:因GALNTL5属于较少研究的糖基转移酶家族成员,相关文献有限,以上内容基于类似主题文献整合,实际研究中建议通过PubMed或Web of Science以“GALNTL5”和“recombinant”为关键词进一步检索近期发表论文。
Recombinant human GALNTL5 (Polypeptide N-Acetylgalactosaminyltransferase-Like 5) is a glycosyltransferase involved in O-linked protein glycosylation, a post-translational modification critical for protein stability, localization, and function. Belonging to the GALNT family, GALNTL5 transfers N-acetylgalactosamine (GalNAc) to serine or threonine residues, initiating mucin-type glycosylation. While most GALNTs are membrane-bound, GALNTL5 lacks a transmembrane domain and is predicted to be secreted, suggesting distinct regulatory roles. It is highly expressed in testis and heart tissues, with emerging links to fertility and muscle-related functions. Dysregulation of GALNTL5 has been observed in muscular dystrophy and cancers, potentially serving as a biomarker or therapeutic target. Recombinant GALNTL5 is produced via mammalian or insect cell systems to ensure proper folding and glycosylation. Its recombinant form enables structural studies, substrate screening, and functional investigations into glycosylation mechanisms. Current research focuses on characterizing its enzymatic specificity, tissue-specific roles, and involvement in diseases. The protein’s unique secretory nature and tissue expression profile make it a subject of interest for understanding atypical glycosylation pathways and developing diagnostic or therapeutic tools.
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