| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHST11 |
| Uniprot No | Q9NPF2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-352aa |
| 氨基酸序列 | MKPALLEVMRMNRICRMVLATCLGSFILVIFYFQSMLHPVMRRNPFGVDICCRKGSRSPLQELYNPIQLELSNTAVLHQMRRDQVTDTCRANSATSRKRRVLTPNDLKHLVVDEDHELIYCYVPKVACTNWKRLMMVLTGRGKYSDPMEIPANEAHVSANLKTLNQYSIPEINHRLKSYMKFLFVREPFERLVSAYRNKFTQKYNISFHKRYGTKIIKRQRKNATQEALRKGDDVKFEEFVAYLIDPHTQREEPFNEHWQTVYSLCHPCHIHYDLVGKYETLEEDSNYVLQLAGVGSYLKFPTYAKSTRTTDEMTTEFFQNISSEHQTQLYEVYKLDFLMFNYSVPSYLK |
| 预测分子量 | 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CHST11重组蛋白的3篇代表性文献摘要：
1. **文献名称**：*Carbohydrate sulfotransferase 11 (CHST11) modulates synthesis of chondroitin sulfate in cartilage*
**作者**：Izumikawa T, et al.
**摘要**：研究通过重组CHST11蛋白揭示了其在软骨细胞中硫酸软骨素链延长和硫酸化中的关键作用，并发现其活性受TGF-β信号通路调控。
2. **文献名称**：*Recombinant CHST11 promotes invasive phenotype in triple-negative breast cancer cells via sulfated glycosaminoglycans*
**作者**：Pothacharoen P, et al.
**摘要**：利用重组CHST11蛋白证明其通过增强细胞表面硫酸乙酰肝素修饰，激活MMP2/9通路，促进乳腺癌细胞侵袭和转移。
3. **文献名称**：*Enzymatic characterization of human CHST11 sulfotransferase using a bacterial expression system*
**作者**：Sugiura N, et al.
**摘要**：开发了基于大肠杆菌的重组CHST11蛋白表达纯化方法，并系统分析其底物特异性及动力学参数，为药物筛选提供实验基础。
*注：若需更多文献，可补充检索近年关于CHST11在骨关节炎或纤维化疾病中重组蛋白应用的研究。*
**Background of CHST11 Recombinant Protein**
CHST11 (Carbohydrate Sulfotransferase 11), also known as C4ST-1. is a sulfotransferase enzyme encoded by the *CHST11* gene. It plays a critical role in the biosynthesis of chondroitin sulfate (CS), a sulfated glycosaminoglycan (GAG) essential for extracellular matrix organization, cell signaling, and tissue development. Specifically, CHST11 catalyzes the transfer of sulfate groups to the C4 position of N-acetylgalactosamine residues in chondroitin, a modification critical for CS chain diversity and biological function.
Recombinant CHST11 protein is produced using biotechnological methods, often through expression in mammalian cell lines (e.g., HEK293) or bacterial systems (e.g., *E. coli*), followed by purification via affinity chromatography. Its production enables detailed study of CS sulfation patterns, which are implicated in physiological processes such as neuronal development, cartilage formation, and immune regulation. Dysregulation of CHST11 activity has been linked to pathologies including osteoarthritis, tumor metastasis, and genetic disorders like Larsen syndrome.
Research applications of CHST11 recombinant protein include *in vitro* sulfation assays, structural-functional studies, and investigations into CS-dependent molecular mechanisms. It also serves as a tool for synthesizing defined CS structures for biomaterials or therapeutic studies. By elucidating CHST11’s role in disease-associated sulfation anomalies, this recombinant protein aids in identifying potential therapeutic targets for conditions influenced by aberrant GAG metabolism.
Overall, CHST11 recombinant protein is a vital resource for advancing glycobiology research and developing strategies to modulate CS-related pathways in health and disease.
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