纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | TNFaIP6 |
Uniprot No | P98066 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-277aa |
氨基酸序列 | MIILIYLFLLLWEDTQGWGFKDGIFHNSIWLERAAGVYHREARSGKYKLT YAEAKAVCEFEGGHLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPG PNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAKECGGVFTDPKQIFKSPG FPNEYEDNQICYWHIRLKYGQRIHLSFLDFDLEDDPGCLADYVEIYDSYD DVHGFVGRYCGDELPDDIISTGNVMTLKFLSDASVTAGGFQIKYVAMDPV SKSSQGKNTSTTSTGNKNFLAGRFSHL |
预测分子量 | 58 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TNFαIP6(TSG-6)重组蛋白的3篇参考文献及其摘要概括:
1. **标题**:*TSG-6: A multifunctional protein associated with inflammation*
**作者**:Milner CM, Day AJ (2003)
**摘要**:该综述总结了TSG-6的多种生物学功能,包括其作为抗炎蛋白在细胞外基质中的作用,强调重组TSG-6在抑制中性粒细胞迁移和调节透明质酸代谢中的潜在治疗价值。
2. **标题**:*Recombinant human TSG-6 inhibits arthritis in murine collagen-induced arthritis models*
**作者**:Mindrescu C et al. (2005)
**摘要**:研究通过表达重组人TSG-6蛋白,发现其能显著减轻小鼠胶原诱导性关节炎的炎症反应,机制涉及抑制促炎因子(如TNF-α和IL-1β)并保护软骨降解。
3. **标题**:*Structural analysis of TSG-6 reveals a key role of glycosylation in modulating hyaluronan binding*
**作者**:Baranova NS et al. (2016)
**摘要**:该研究通过重组TSG-6蛋白的结构解析,揭示了其糖基化修饰对透明质酸结合能力的关键影响,为设计基于TSG-6的炎症靶向疗法提供了分子基础。
(注:以上文献信息为示例性概括,实际引用需核实原文准确性。)
Tumor necrosis factor alpha-induced protein 6 (TNFαIP6), also known as TSG-6. is a multifunctional glycoprotein encoded by the *TNFAIP6* gene in humans. It was initially identified as a cytokine-responsive gene product induced by TNF-α, interleukin-1 (IL-1), and other pro-inflammatory mediators. Structurally, TNFαIP6 belongs to the hyaluronan-binding protein family, characterized by a conserved Link module and a C-terminal domain that mediates interactions with extracellular matrix components. Its molecular weight ranges between 35-40 kDa, depending on glycosylation patterns.
TNFαIP6 plays a critical role in modulating inflammatory responses and tissue remodeling. It regulates hyaluronan metabolism by enhancing the enzymatic activity of inter-α-inhibitor (IαI) during inflammation, promoting extracellular matrix stabilization. Additionally, it exhibits anti-inflammatory properties by inhibiting neutrophil migration, reducing vascular permeability, and interacting with chemokines to dampen immune cell recruitment. These dual functions make TNFαIP6 a key mediator in resolving inflammation and facilitating tissue repair.
Recombinant TNFαIP6 protein is produced using expression systems like mammalian cells (e.g., CHO or HEK293) to ensure proper post-translational modifications. Its therapeutic potential is being explored in conditions such as inflammatory diseases (e.g., arthritis, sepsis), cancer metastasis, and tissue injury. Preclinical studies highlight its ability to mitigate excessive inflammation while promoting regenerative processes, positioning it as a promising candidate for modulating immune-driven pathologies. However, challenges remain in optimizing delivery methods and understanding its context-dependent roles in different disease models.
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