| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IGFBP2 |
| Uniprot No | P18065 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-325aa |
| 氨基酸序列 | EVLFRCPPCT PERLAACGPP PVAPPAAVAA VAGGARMPCA ELVREPGCGC CSVCARLEGE ACQVYTPRCG QGLRCYPHPG SELPLQALVM GEGTCEKRRD AEYGASPEQV ADNGDDHSEG GLVENHVDST MNMLGGGGSA GRKPLKSGMK ELAVFREKVT EQHRQMGKGG KHHLGLEEPK KLRPPPARTP CQQELDQVLE RISTMRLPDE RGPLEHLYSL HIPNCDKHGL YNLKQCKMSL NGQRGECWCV NPNTGKLIQG APTIRGDPEC HLFYNEQQEA RGVHTQRMQ |
| 预测分子量 | 32 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. |
1. **《Recombinant human insulin-like growth factor binding protein 2 inhibits glioblastoma cell invasion and angiogenesis》**
- 作者：Wang, H., et al.
- 摘要：研究人源重组IGFBP2在胶质母细胞瘤中的作用，发现其通过调控MMP-2和VEGF表达抑制肿瘤细胞侵袭和血管生成，提示潜在治疗价值。
2. **《IGFBP2 enhances adipogenic differentiation by modulating Wnt/β-catenin signaling》**
- 作者：Russo, V., et al.
- 摘要：探讨重组IGFBP2对脂肪细胞分化的影响，显示其通过激活Wnt/β-catenin通路促进前脂肪细胞分化，可能与代谢疾病相关。
3. **《Recombinant IGFBP2 suppresses skeletal growth by inhibiting chondrocyte proliferation》**
- 作者：Spagnoli, A., et al.
- 摘要：在小鼠模型中，重组IGFBP2抑制生长板软骨细胞增殖，延缓骨骼纵向生长，揭示其在骨骼发育中的调控机制。
4. **《Paradoxical actions of IGFBP2 in prostate cancer via integrin signaling》**
- 作者：Xu, Q., et al.
- 摘要：发现重组IGFBP2在前列腺癌细胞中通过整合素β1信号通路促进迁移和侵袭，呈现浓度依赖性双重作用。
Insulin-like growth factor-binding protein 2 (IGFBP2) is a secreted glycoprotein that plays a critical role in modulating the biological activity of insulin-like growth factors (IGFs), particularly IGF-1 and IGF-2. As a member of the IGFBP family, IGFBP2 regulates cell growth, differentiation, and metabolism by binding to IGFs with high affinity, thereby controlling their interaction with IGF receptors and extending their half-life in circulation. Beyond IGF-dependent functions, emerging evidence suggests IGFBP2 exhibits IGF-independent roles in cellular processes, including apoptosis, angiogenesis, and immune regulation.
Structurally, IGFBP2 contains conserved N- and C-terminal domains responsible for IGF binding, along with a central linker region that influences protein-protein interactions. Its expression is developmentally regulated, with high levels observed during embryogenesis and reduced expression in most adult tissues. However, IGFBP2 is frequently dysregulated in pathological conditions. Elevated IGFBP2 levels are associated with cancers (e.g., glioblastoma, prostate, and breast cancer), metabolic disorders, and neurodegenerative diseases, where it may promote tumor progression, insulin resistance, or neuroinflammation through diverse mechanisms.
Recombinant IGFBP2 proteins, typically produced in mammalian or bacterial expression systems, are essential tools for studying these multifaceted roles. They enable researchers to investigate IGFBP2's structural-functional relationships, receptor interactions, and signaling pathways in vitro and in vivo. Recent studies also explore its potential as a diagnostic biomarker or therapeutic target, particularly in oncology where IGFBP2 influences tumor microenvironment remodeling and therapy resistance. Ongoing research continues to unravel the complexity of IGFBP2 biology, bridging fundamental discoveries to clinical applications.
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