| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | XYLT1 |
| Uniprot No | Q86Y38 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-959aa |
| 氨基酸序列 | MVAAPCARRLARRSHSALLAALTVLLLQTLVVWNFSSLDSGAGERRGGAAVGGGEQPPPAPAPRRERRDLPAEPAAARGGGGGGGGGGGGRGPQARARGGGPGEPRGQQPASRGALPARALDPHPSPLITLETQDGYFSHRPKEKVRTDSNNENSVPKDFENVDNSNFAPRTQKQKHQPELAKKPPSRQKELLKRKLEQQEKGKGHTFPGKGPGEVLPPGDRAAANSSHGKDVSRPPHARKTGGSSPETKYDQPPKCDISGKEAISALSRAKSKHCRQEIGETYCRHKLGLLMPEKVTRFCPLEGKANKNVQWDEDSVEYMPANPVRIAFVLVVHGRASRQLQRMFKAIYHKDHFYYIHVDKRSNYLHRQVLQVSRQYSNVRVTPWRMATIWGGASLLSTYLQSMRDLLEMTDWPWDFFINLSAADYPIRTNDQLVAFLSRYRDMNFLKSHGRDNARFIRKQGLDRLFLECDAHMWRLGDRRIPEGIAVDGGSDWFLLNRRFVEYVTFSTDDLVTKMKQFYSYTLLPAESFFHTVLENSPHCDTMVDNNLRITNWNRKLGCKCQYKHIVDWCGCSPNDFKPQDFHRFQQTARPTFFARKFEAVVNQEIIGQLDYYLYGNYPAGTPGLRSYWENVYDEPDGIHSLSDVTLTLYHSFARLGLRRAETSLHTDGENSCRYYPMGHPASVHLYFLADRFQGFLIKHHATNLAVSKLETLETWVMPKKVFKIASPPSDFGRLQFSEVGTDWDAKERLFRNFGGLLGPMDEPVGMQKWGKGPNVTVTVIWVDPVNVIAATYDILIESTAEFTHYKPPLNLPLRPGVWTVKILHHWVPVAETKFLVAPLTFSNRQPIKPEEALKLHNGPLRNAYMEQSFQSLNPVLSLPINPAQVEQARRNAASTGTALEGWLDSLVGGMWTAMDICATGPTACPVMQTCSQTAWSSFSPDPKSELGAVKPDGRLR |
| 预测分子量 | 107,5 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XYLT1重组蛋白的示例参考文献(内容为模拟生成，建议通过学术数据库验证准确性)：
1. **"Functional characterization of recombinant human XYLT1 in glycosaminoglycan biosynthesis"**
*作者：Smith A, et al.*
摘要：研究通过昆虫细胞系统表达重组人XYLT1蛋白，证实其在体外催化木糖转移至核心蛋白的活性，并分析其酶动力学参数。
2. **"Expression and purification of XYLT1 in a mammalian cell system for structural studies"**
*作者：Zhang L, et al.*
摘要：报道在HEK293细胞中表达并纯化功能性重组XYLT1.利用结晶学初步解析其结构，揭示底物结合域的关键氨基酸残基。
3. **"Role of recombinant XYLT1 in modulating TGF-β signaling in fibroblast cultures"**
*作者：Jones R, et al.*
摘要：通过大肠杆菌表达系统获得重组XYLT1.证明其添加可增强细胞外基质的合成，并调控TGF-β通路相关基因表达。
4. **"High-yield production of XYLT1 in Pichia pastoris and its application in disease modeling"**
*作者：Wang H, et al.*
摘要：利用毕赤酵母系统实现重组XYLT1的高效分泌表达，并应用于埃勒斯-当洛综合征细胞模型中，验证其功能恢复潜力。
建议通过PubMed或Google Scholar检索最新文献，以获取真实研究数据。
XYLT1 (Xylosyltransferase 1) is a key enzyme involved in the biosynthesis of proteoglycans, essential components of the extracellular matrix (ECM). It catalyzes the initial step in glycosaminoglycan (GAG) chain formation by transferring xylose residues to specific serine residues on core proteins, a critical process for ECM assembly and cell signaling. The recombinant XYLT1 protein, produced through genetic engineering in systems like mammalian cells or bacteria, enables researchers to study its enzymatic activity, structure-function relationships, and regulatory mechanisms in vitro.
Structurally, XYLT1 contains a conserved glycosyltransferase domain and substrate-binding regions critical for its catalytic function. Mutations in the XYLT1 gene are linked to human disorders such as Desbuquois dysplasia and connective tissue abnormalities, highlighting its role in skeletal development and tissue homeostasis. Recombinant XYLT1 is particularly valuable for investigating diseases associated with GAG deficiency, including osteoarthritis, fibrosis, and certain cancers where ECM remodeling drives metastasis. Additionally, it serves as a tool for screening potential therapeutic agents targeting proteoglycan synthesis pathways. Recent studies also explore its involvement in modulating growth factor signaling (e.g., FGF, TGF-β) through heparan sulfate proteoglycan interactions. The production of active recombinant XYLT1 remains challenging due to its transmembrane domain and post-translational modification requirements, driving ongoing optimization of expression systems to enhance yield and functionality for both basic research and biotechnological applications.
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