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| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VEGFB |
| Uniprot No | P49765 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-207aa |
| 氨基酸序列 | PVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHSQCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAPSTTSALTPGPAAAAADAAASSVAKGGA |
| 预测分子量 | 54.5 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VEGFB重组蛋白的参考文献，涵盖其功能及疾病相关研究：
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1. **文献名称**: *VEGF-B promotes endothelial fatty acid uptake via fatty acid transporter FAT/CD36*
**作者**: Hagberg CE, et al.
**摘要**: 该研究发现重组VEGF-B蛋白通过激活VEGFR1/Flt1受体，特异性诱导血管内皮细胞中脂肪酸转运蛋白CD36的表达，从而调控心脏和肌肉组织的脂质代谢，为代谢性疾病治疗提供新靶点。
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2. **文献名称**: *Therapeutic potential of VEGF-B in coronary artery disease: Mechanisms and preclinical evidence*
**作者**: Robciuc MR, et al.
**摘要**: 研究利用重组VEGF-B蛋白在小鼠心肌缺血模型中验证其促血管新生作用，发现其通过激活VEGFR1/Neuropilin-1信号通路改善心脏血流灌注，且未引起病理性血管渗漏，提示其治疗缺血性心脏病的潜力。
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3. **文献名称**: *Recombinant VEGF-B186 attenuates apoptosis and inflammation in diabetic retinopathy models*
**作者**: Li X, et al.
**摘要**: 该研究证明重组人源VEGF-B186蛋白可通过抑制视网膜内皮细胞凋亡和减少炎症因子IL-6/TNF-α释放，缓解糖尿病小鼠视网膜病变，提示VEGF-B可能作为糖尿病并发症的新型治疗分子。
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如需更详细文献信息(期刊、年份等)，可进一步补充关键词或研究背景。
Vascular endothelial growth factor B (VEGFB) is a member of the VEGF protein family, which plays critical roles in angiogenesis and vascular biology. Discovered in the 1990s, VEGFB shares structural homology with VEGF-A but exhibits distinct functional characteristics. It is encoded by the *VEGFB* gene in humans and exists as two main splice isoforms (VEGFB167 and VEGFB186) that differ in their heparin-binding domains. Unlike VEGF-A, VEGFB shows limited angiogenic activity but is highly expressed in metabolically active tissues such as the heart, skeletal muscle, and brown adipose tissue. This tissue-specific expression hints at its unique role in regulating lipid metabolism and energy homeostasis.
Recombinant VEGFB is produced using biotechnological platforms (e.g., bacterial, mammalian, or yeast expression systems) to generate purified, bioactive proteins for research and therapeutic applications. Its structure typically includes a homodimer stabilized by disulfide bonds, with post-translational modifications like glycosylation depending on the production system. Recombinant VEGFB binds preferentially to VEGF receptor 1 (VEGFR1/Flt-1) and neuropilin-1 (NRP-1), activating downstream signaling pathways such as PKC-ERK1/2. which influence cellular survival and metabolic regulation rather than traditional angiogenic responses.
Current studies focus on VEGFB's therapeutic potential in cardiovascular diseases, metabolic disorders, and cancer. In preclinical models, it has shown promise in improving coronary collateral circulation in ischemic heart disease and enhancing fatty acid uptake in diabetic conditions. However, its weak angiogenic properties and complex crosstalk with VEGF-A pathways present challenges for clinical translation. Research also explores its role in modulating inflammation and tissue repair. Despite being less characterized than other VEGF members, recombinant VEGFB remains a valuable tool for dissecting metabolic-vascular interactions and developing targeted therapies with fewer side effects compared to VEGF-A-based approaches. Ongoing efforts aim to optimize delivery systems and clarify its tissue-specific signaling mechanisms.
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