| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EXTL3 |
| Uniprot No | O43909 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-919aa |
| 氨基酸序列 | MTGYTMLRNGGAGNGGQTCMLRWSNRIRLTWLSFTLFVILVFFPLIAHYYLTTLDEADEAGKRIFGPRVGNELCEVKHVLDLCRIRESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQPKLSLPIRLLPEKDDAGLPPPKATRGCRLHNCFDYSRCPLTSGFPVYVYDSDQFVFGSYLDPLVKQAFQATARANVYVTENADIACLYVILVGEMQEPVVLRPAELEKQLYSLPHWRTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVAQSTFYTVQYRPGFDLVVSPLVHAMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEARSFEEEMEGDPPADYDDRIIATLKAVQDSKLDQVLVEFTCKNQPKPSLPTEWALCGEREDRLELLKLSTFALIITPGDPRLVISSGCATRLFEALEVGAVPVVLGEQVQLPYQDMLQWNEAALVVPKPRVTEVHFLLRSLSDSDLLAMRRQGRFLWETYFSTADSIFNTVLAMIRTRIQIPAAPIREEAAAEIPHRSGKAAGTDPNMADNGDLDLGPVETEPPYASPRYLRNFTLTVTDFYRSWNCAPGPFHLFPHTPFDPVLPSEAKFLGSGTGFRPIGGGAGGSGKEFQAALGGNVPREQFTVVMLTYEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRTEKNSLNNRFLPWNEIETEAILSIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDIPHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAIRDMVDEYINCEDIAMNFLVSHITRKPPIKVTSRWTFRCPGCPQALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRVDSVLFKTRLPHDKTKCFKFI |
| 分子量 | 131.1 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EXTL3蛋白的3篇代表性文献概览(文献标题及内容为示例性说明，可能不直接对应真实出版物)：
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1. **文献名称**: **"Crystal structure of human EXTL3 provides insight into heparan sulfate biosynthesis"**
**作者**: Yamamoto S, et al.
**摘要**: 本研究解析了重组人EXTL3蛋白的晶体结构，揭示了其催化结构域的构象及与底物结合的机制，阐明了EXTL3在硫酸乙酰肝素(HSPG)链延伸中的关键酶活性。
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2. **文献名称**: **"EXTL3 mutations cause skeletal dysplasia and immune dysregulation via defective HS chain synthesis"**
**作者**: Chen L, et al.
**摘要**: 通过重组EXTL3蛋白功能实验，发现其突变导致HSPG合成缺陷，进而影响BMP/FGF信号通路，解释了患者骨骼发育异常和免疫失调的分子机制。
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3. **文献名称**: **"Recombinant EXTL3 as a therapeutic target suppresses tumor angiogenesis in colorectal cancer"**
**作者**: Wang Y, et al.
**摘要**: 研究利用重组人EXTL3蛋白进行体外实验，发现其过表达通过调节VEGF信号通路抑制肿瘤血管生成，提示EXTL3作为癌症治疗的潜在靶点。
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**注**：以上文献为示例性内容，实际研究需以具体数据库(如PubMed、ScienceDirect)检索为准。如需真实文献，建议通过关键词“EXTL3 protein recombinant”或“EXTL3 heparan sulfate”查询最新论文。
Here’s a concise overview of recombinant human EXTL3 protein:
Recombinant human EXTL3 protein is a biologically engineered form of the EXTL3 (exostosin-like glycosyltransferase 3) protein, a member of the EXT family of glycosyltransferases. Naturally, EXTL3 plays a critical role in heparan sulfate (HS) and heparin biosynthesis by catalyzing the addition of alternating glucuronic acid and N-acetylglucosamine residues during heparan sulfate proteoglycan (HSPG) chain elongation. Its structural features include two distinct glycosyltransferase domains (GT64 and GT47), enabling specific catalytic functions in the biosynthetic pathway.
The recombinant version is produced via heterologous expression systems (e.g., mammalian cells or bacteria) to study its enzymatic activity, structural properties, and interactions. This engineered protein retains functional domains while offering advantages like high purity and scalability for research applications. Studies utilizing recombinant EXTL3 have advanced our understanding of HSPG-mediated processes, including cell signaling, extracellular matrix organization, and pathogen interactions.
EXTL3 dysregulation has been implicated in developmental disorders and cancers, making the recombinant protein valuable for investigating disease mechanisms and screening therapeutic agents. Recent research highlights its potential role in modulating Wnt/β-catenin signaling and fibroblast growth factor (FGF) responses, emphasizing its biological significance beyond HS synthesis. Recombinant EXTL3 continues to serve as an essential tool for both basic science and translational studies.
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