纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | CHST10 |
Uniprot No | O43529 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 28-356aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN |
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CHST10重组蛋白的3篇参考文献的示例(注:以下内容为虚构示例,仅供格式参考):
1. **《重组CHST10蛋白在昆虫细胞中的表达及酶活性分析》**
- 作者:Zhang L, et al.
- 摘要:本研究通过杆状病毒-昆虫细胞系统成功表达并纯化了重组CHST10蛋白,证实其具有硫酸转移酶活性,可催化硫酸基团向特定糖链底物的转移。
2. **《CHST10通过调节硫酸乙酰肝素修饰影响肿瘤细胞迁移的机制研究》**
- 作者:Wang Y, et al.
- 摘要:利用重组CHST10蛋白进行体外实验,发现其通过介导硫酸乙酰肝素的磺酸化修饰,抑制乳腺癌细胞的侵袭和迁移能力。
3. **《CHST10蛋白的晶体结构解析及其底物结合位点鉴定》**
- 作者:Smith J, et al.
- 摘要:通过X射线晶体学解析了重组CHST10蛋白的三维结构,揭示了其催化活性中心的关键氨基酸残基及底物特异性结合的分子机制。
(提示:实际文献需通过PubMed、Web of Science等平台检索确认。)
CHST10 (Carbohydrate Sulfotransferase 10) is a member of the sulfotransferase family that catalyzes the transfer of sulfate groups to carbohydrate moieties, particularly during the biosynthesis of glycosaminoglycans (GAGs) like chondroitin sulfate. This enzyme plays a critical role in post-translational modifications, influencing cell signaling, extracellular matrix organization, and cellular interactions. The CHST10 gene encodes a type II transmembrane protein localized to the Golgi apparatus, where it sulfates specific hydroxyl positions on chondroitin, modulating GAG structure and function.
Recombinant CHST10 protein is produced using heterologous expression systems (e.g., E. coli, mammalian cells) to enable functional studies. Its production typically involves cloning the CHST10 coding sequence into expression vectors, followed by purification via affinity chromatography. The recombinant form retains enzymatic activity, allowing researchers to investigate substrate specificity, kinetic properties, and regulatory mechanisms. It serves as a tool to explore sulfation patterns in physiological processes, including neural development, cartilage formation, and immune response modulation.
Studies implicate CHST10 in diseases such as cancer metastasis, where altered GAG sulfation affects cell adhesion and invasion. Neurodegenerative conditions like Alzheimer’s disease have also been linked to CHST10-mediated sulfation changes in brain proteoglycans. Recombinant CHST10 facilitates drug discovery by screening inhibitors or activators targeting sulfation pathways. Current research focuses on its tissue-specific roles and therapeutic potential, though mechanistic details remain partially unexplored. This protein’s study bridges glycobiology and disease pathology, offering insights into precision therapies targeting sulfation-dependent cellular processes.
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