| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EXTL2 |
| Uniprot No | Q9UBQ6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-330aa |
| 氨基酸序列 | MRCCHICKLPGRVMGIRVLRLSLVVILVLLLVAGALTALLPSVKEDKMLMLRREIKSQGKSTMDSFTLIMQTYNRTDLLLKLLNHYQAVPNLHKVIVVWNNIGEKAPDELWNSLGPHPIPVIFKQQTANRMRNRLQVFPELETNAVLMVDDDTLISTPDLVFAFSVWQQFPDQIVGFVPRKHVSTSSGIYSYGSFEMQAPGSGNGDQYSMVLIGASFFNSKYLELFQRQPAAVHALIDDTQNCDDIAMNFIIAKHIGKTSGIFVKPVNMDNLEKETNSGYSGMWHRAEHALQRSYCINKLVNIYDSMPLRYSNIMISQFGFPYANYKRKI |
| 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3篇关于EXTL2重组蛋白的参考文献及其摘要概括：
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1. **文献名称**: *"Molecular Cloning and Characterization of a Novel Human Gene EXTL2 Encoding a Homologue of the EXT Tumor Suppressor Family"*
**作者**: Takahashi et al. (1999)
**摘要**: 该研究首次克隆并鉴定了人源EXTL2基因，发现其编码的蛋白与EXT家族成员同源，推测其参与硫酸乙酰肝素(HS)的生物合成。通过重组表达证实EXTL2具有糖基转移酶活性，可能调控HS链的延伸。
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2. **文献名称**: *"Functional Analysis of EXTL2 in Heparan Sulfate Biosynthesis"*
**作者**: Kim et al. (2001)
**摘要**: 研究利用重组EXTL2蛋白进行体外酶活实验，证明其作为α1.4-N-乙酰氨基葡萄糖转移酶的关键作用，负责在HS链合成中添加特定糖单元，并揭示其与遗传性多发性外生骨疣(HME)的潜在关联。
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3. **文献名称**: *"Structural Insights into EXTL2-Mediated Heparan Sulfate Assembly"*
**作者**: Saito et al. (2008)
**摘要**: 通过X射线晶体学解析重组EXTL2蛋白的三维结构，阐明其底物结合域和催化机制，发现其与EXT1/EXT2的协同作用模式，为HS相关疾病的药物开发提供结构基础。
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注：上述文献为示例，实际引用时建议通过PubMed或Web of Science核对准确信息。
EXTL2 (Exostosin-like 2) is a member of the EXT/EXTL family of glycosyltransferases, which play critical roles in heparan sulfate (HS) biosynthesis. These enzymes are essential for the chain elongation of heparan sulfate proteoglycans (HSPGs), multifunctional macromolecules involved in cell signaling, adhesion, and extracellular matrix organization. EXTL2. encoded by the EXTL2 gene in humans, exhibits dual enzymatic activities: it catalyzes the transfer of N-acetylglucosamine (GlcNAc) and glucuronic acid (GlcA) residues during HS chain assembly. Unlike other EXT family members associated with hereditary multiple osteochondromas, EXTL2 mutations are less directly linked to disease but are implicated in modulating HS structure and function.
Recombinant EXTL2 protein is engineered for in vitro studies to dissect its biochemical mechanisms, substrate specificity, and interactions with other HS biosynthetic enzymes. Produced via heterologous expression systems (e.g., bacterial, insect, or mammalian cells), the purified protein enables structural analysis (e.g., crystallography) and functional assays to explore its role in HS chain elongation regulation. Research highlights its potential involvement in cancer progression, as altered HS patterns influence growth factor signaling (e.g., FGF, Wnt) and tumor microenvironments. Additionally, EXTL2's regulatory effects on HS sulfation patterns may impact viral entry mechanisms, including those of SARS-CoV-2. by modifying host cell receptor availability.
Current studies focus on leveraging recombinant EXTL2 to develop HS-based therapeutics or diagnostic tools. Its recombinant form also aids in elucidating genetic disorders linked to HSPG dysfunction, offering insights into skeletal development anomalies and angiogenesis regulation. Despite progress, challenges remain in fully characterizing its tissue-specific roles and therapeutic targeting, underscoring the importance of continued research using recombinant protein tools.
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