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纯度 | >97%SDS-PAGE. |
种属 | Human |
靶点 | Cxcl12 |
Uniprot No | P48061 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 22-89aa |
氨基酸序列 | KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK |
预测分子量 | 8.0 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CXCL12(SDF-1)重组蛋白的参考文献及其摘要概括:
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1. **文献名称**: *"The chemokine SDF-1 is a chemoattractant for human CD34+ hematopoietic progenitor cells"*
**作者**: Aiuti A. et al. (1997)
**摘要**: 该研究首次证明重组人CXCL12(SDF-1)蛋白对CD34+造血干/祖细胞具有趋化活性,揭示了其在造血干细胞归巢和骨髓微环境调控中的关键作用。
2. **文献名称**: *"CXCL12/CXCR4 axis in cancer stem cell migration and metastasis"*
**作者**: Kato H. et al. (2020)
**摘要**: 文章综述了重组CXCL12蛋白通过激活CXCR4受体介导的信号通路,促进肿瘤干细胞迁移和转移的机制,强调了其在癌症治疗中的潜在靶点价值。
3. **文献名称**: *"Recombinant SDF-1α protein enhances angiogenesis and tissue regeneration in ischemic injury models"*
**作者**: Ceradini D.J. et al. (2004)
**摘要**: 研究利用重组SDF-1α蛋白在小鼠缺血模型中验证其促血管生成作用,表明其通过招募内皮祖细胞促进组织修复,为缺血性疾病治疗提供新策略。
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以上文献均聚焦于重组CXCL12蛋白的生物学功能,涵盖干细胞调控、癌症转移及组织再生等领域。如需具体文献链接或补充信息,可进一步说明。
Chemokine (C-X-C motif) ligand 12 (Cxcl12), also known as stromal cell-derived factor-1 (SDF-1), is a small signaling protein belonging to the chemokine family. It exists as two primary isoforms, Cxcl12α and Cxcl12β, produced through alternative splicing. Cxcl12 interacts with its cognate receptor Cxcr4 and the atypical receptor Cxcr7. regulating diverse biological processes, including hematopoietic stem cell homing, neurogenesis, immune cell trafficking, and embryonic development. Its structure features a conserved chemokine domain with characteristic cysteine residues critical for receptor binding and signaling.
Recombinant Cxcl12 is engineered using expression systems like *E. coli* or mammalian cells, followed by purification via chromatography to ensure high bioactivity and low endotoxin levels. This allows precise control over protein concentration and consistency, making it invaluable for *in vitro* and *in vivo* studies. Researchers utilize recombinant Cxcl12 to investigate mechanisms of cell migration, tissue regeneration, and cancer metastasis, as the Cxcr4/Cxcl12 axis is implicated in tumor cell proliferation, invasion, and chemoresistance. In therapeutic contexts, Cxcl12 analogs or antagonists (e.g., AMD3100) are explored for targeting cancers, inflammatory diseases, or enhancing stem cell mobilization.
Additionally, Cxcl12 plays a role in cardiovascular and neurological repair, promoting angiogenesis and neuronal survival. Its recombinant form is essential for developing organoid models and drug screening platforms. Despite its physiological importance, dysregulated Cxcl12 signaling contributes to pathological conditions, underscoring the need for targeted therapies. Overall, recombinant Cxcl12 remains a critical tool for dissecting chemokine biology and advancing regenerative and anti-cancer strategies.
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