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| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Vaspin |
| Uniprot No | Q8IW75 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-414aa |
| 氨基酸序列 | LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK |
| 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. |
以下是关于Vaspin重组蛋白的3篇代表性文献，包含文献名称、作者及摘要概括：
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1. **文献名称**: *Serum Vaspin Levels Are Associated with Insulin Sensitivity in Obese Individuals*
**作者**: Hida K, et al.
**摘要**: 该研究首次报道Vaspin作为内脏脂肪组织分泌的丝氨酸蛋白酶抑制剂，通过重组蛋白实验证实其可改善肥胖小鼠的胰岛素敏感性，并抑制脂肪组织炎症反应，提示其在代谢综合征中的潜在治疗作用。
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2. **文献名称**: *Recombinant Vaspin Attenuates Oxidative Stress and Inflammation via AMPK/NF-κB Signaling in Endothelial Cells*
**作者**: Li Q, et al.
**摘要**: 研究利用重组Vaspin蛋白处理内皮细胞，发现其通过激活AMPK通路抑制NF-κB介导的炎症因子释放，并减轻氧化应激损伤，为Vaspin在动脉粥样硬化中的保护机制提供了实验依据。
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3. **文献名称**: *Production and Functional Characterization of Recombinant Human Vaspin in a Prokaryotic System*
**作者**: Zhang Y, et al.
**摘要**: 该研究成功在大肠杆菌中表达并纯化具有生物活性的重组人Vaspin蛋白，通过体外实验验证其抑制丝氨酸蛋白酶活性及调节脂肪细胞分化的功能，为大规模制备研究级Vaspin蛋白提供了方法学支持。
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如需具体文献来源或更多研究方向(如临床前应用、结构解析等)，可进一步补充说明!
**Background of Vaspin Recombinant Protein**
Vaspin (visceral adipose tissue-derived serpin), also known as SERPINA12. is an adipokine initially identified in 2005 in a rat model of obesity and type 2 diabetes. It belongs to the serine protease inhibitor (serpin) family and is predominantly secreted by visceral adipose tissue, though its expression has been detected in other tissues, including liver, pancreas, and skin. Vaspin gained attention due to its potential role in metabolic regulation, particularly in obesity-associated insulin resistance and glucose homeostasis. Studies suggest it functions as an endogenous compensatory molecule, counteracting metabolic disturbances linked to adipose tissue dysfunction.
Structurally, vaspin is a ~40–45 kDa protein that inhibits proteolytic enzymes, particularly kallikrein 7 (KLK7), which may influence pathways related to inflammation, fibrinolysis, and extracellular matrix remodeling. Its recombinant form is produced via genetic engineering in bacterial, yeast, or mammalian expression systems, enabling standardized studies on its biological activities. Recombinant vaspin retains the functional epitopes of the native protein, allowing researchers to explore its therapeutic potential in metabolic disorders, cardiovascular diseases, and chronic inflammation.
Preclinical studies highlight vaspin’s anti-inflammatory and insulin-sensitizing effects. For instance, it improves glucose tolerance, reduces pro-inflammatory cytokine levels, and protects pancreatic β-cells in rodent models. However, its mechanisms remain partially unclear, with proposed pathways involving AMPK/Akt signaling and interactions with adipose-derived hormones like leptin and adiponectin. Challenges in translating these findings include understanding tissue-specific effects, dose-dependent responses, and potential off-target interactions.
Despite unresolved questions, vaspin recombinant protein remains a promising candidate for biomarker development and therapeutic targeting in metabolic syndrome. Ongoing research focuses on clarifying its physiological roles, optimizing recombinant production for clinical use, and exploring its diagnostic value in human obesity and diabetes.
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