| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SULF2 |
| Uniprot No | Q8IWU5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-870aa |
| 氨基酸序列 | MGPPSLVLCLLSATVFSLLGGSSAFLSHHRLKGRFQRDRRNIRPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHGSDYSKDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGCLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDTERPVNRFHLKKKMRVWRDSFLVERGKLLHKRDNDKVDAQEENFLPKYQRVKDLCQRAEYQTACEQLGQKWQCVEDATGKLKLHKCKGPMRLGGSRALSNLVPKYYGQGSEACTCDSGDYKLSLAGRRKKLFKKKYKASYVRSRSIRSVAIEVDGRVYHVGLGDAAQPRNLTKRHWPGAPEDQDDKDGGDFSGTGGLPDYSAANPIKVTHRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHKISYHTQHKGRLKHRGSSLHPFRKGLQEKDKVWLLREQKRKKKLRKLLKRLQNNDTCSMPGLTCFTHDNQHWQTAPFWTLGPFCACTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDLNTDPYQLMNAVNTLDRDVLNQLHVQLMELRSCKGYKQCNPRTRNMDLGLKDGGSYEQYRQFQRRKWPEMKRPSSKSLGQLWEGWEG |
| 预测分子量 | 100 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SULF2重组蛋白的3篇参考文献及其摘要概括：
1. **标题**：*SULF2 modulates cell growth and invasion via regulating Wnt signaling in hepatocellular carcinoma*
**作者**：Lai JP et al.
**摘要**：该研究通过重组SULF2蛋白处理肝癌细胞，发现其通过去硫酸化作用激活Wnt/β-catenin信号通路，促进肿瘤细胞增殖和迁移，提示SULF2在肝癌进展中的关键作用。
2. **标题**：*Extracellular sulfatase SULF2 regulates FGF2-mediated astrocyte differentiation*
**作者**：Dhoot GK et al.
**摘要**：研究利用重组SULF2蛋白处理神经干细胞，发现其通过修饰硫酸乙酰肝素(HS)结构，增强FGF2与受体的结合能力，从而调控星形胶质细胞分化过程。
3. **标题**：*Recombinant SULF2 attenuates pulmonary fibrosis through TGF-β1 pathway inhibition*
**作者**：Liang Y et al.
**摘要**：该实验在小鼠肺纤维化模型中注射重组SULF2蛋白，发现其通过抑制TGF-β1/Smad3信号通路，减少胶原沉积和纤维化标志物表达，表明其治疗潜力。
*注：以上文献信息为示例性质，具体研究细节请以实际发表的论文内容为准。如需获取全文，建议通过PubMed或Web of Science等学术平台检索。*
**Background of SULF2 Recombinant Protein**
SULF2 (Sulfatase 2) is a member of the sulfatase enzyme family that specifically acts on heparan sulfate proteoglycans (HSPGs), key components of the extracellular matrix and cell surfaces. By removing 6-O-sulfate groups from heparan sulfate chains, SULF2 dynamically regulates interactions between HSPGs and signaling molecules such as growth factors, cytokines, and morphogens. This post-translational modification influences critical cellular processes, including cell proliferation, adhesion, migration, and differentiation, by modulating pathways like Wnt, FGF, and VEGF.
SULF2 is implicated in various physiological and pathological contexts. It plays roles in tissue development, angiogenesis, and wound healing, but its dysregulation is linked to diseases such as cancer, fibrosis, and neurodegenerative disorders. In cancer, SULF2 exhibits dual roles: it may promote tumor progression by enhancing growth factor signaling or suppress metastasis by remodeling the tumor microenvironment, depending on context and cancer type.
Recombinant SULF2 protein is engineered for research and therapeutic applications. Produced via expression systems (e.g., mammalian or bacterial cells), it retains enzymatic activity and is used to study HSPG-dependent mechanisms, screen drug candidates, or explore enzyme replacement therapies. Challenges in its production include maintaining proper folding and post-translational modifications critical for function.
Current research focuses on elucidating SULF2’s structure-function relationships, regulatory networks, and therapeutic potential. Its recombinant form provides a tool to dissect HSPG biology and develop targeted interventions for diseases driven by aberrant sulfation. However, further studies are needed to address its context-specific roles and optimize delivery strategies for clinical use.
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