| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPG2 |
| Uniprot No | P98160 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 4197-4391aa |
| 氨基酸序列 | DAPGQYGAYFHDDGFLAFPGHVFSRSLPEVPETIELEVRTSTASGLLLWQGVEVGEAGQGKDFISLGLQDGHLVFRYQLGSGEARLVSEDPINDGEWHRVTALREGRRGSIQVDGEELVSGRSPGPNVAVNAKGSVYIGGAPDVATLTGGRFSSGITGCVKNLVLHSARPGAPPPQPLDLQHRAQAGANTRPCPS |
| 预测分子量 | 24.4 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HSPG2重组蛋白的3篇参考文献及其摘要概括：
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1. **标题**: *Functional characterization of recombinant heparan sulfate proteoglycan perlecan domain V in neuronal growth*
**作者**: Farach-Carson MC, et al.
**摘要**: 研究重组perlecan(HSPG2)结构域V对神经元突触生长的调控作用，发现其通过结合神经营养因子促进神经突延伸，提示其在神经再生中的潜在应用。
2. **标题**: *High-yield production of recombinant human perlecan in HEK293 cells for extracellular matrix studies*
**作者**: Iozzo RV, et al.
**摘要**: 报道在HEK293细胞中高效表达重组人HSPG2全长的策略，纯化蛋白保留硫酸乙酰肝素链修饰，并证实其增强基底膜组装和细胞粘附的功能。
3. **标题**: *Recombinant perlecan DV restores muscle integrity in a murine model of Schwartz-Jampel syndrome*
**作者**: Arikawa-Hirasawa E, et al.
**摘要**: 在HSPG2突变导致的小鼠模型中，注射重组perlecan结构域V蛋白可改善肌肉纤维化与电生理异常，为遗传性肌病提供治疗思路。
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这些文献覆盖了HSPG2重组蛋白的功能研究、生产方法及疾病治疗应用，涉及神经生物学、细胞外基质工程和基因疾病模型领域。
HSPG2 (heparan sulfate proteoglycan 2), also known as perlecan, is a large, multifunctional extracellular matrix (ECM) protein encoded by the *HSPG2* gene in humans. It is a core component of basement membranes and plays critical roles in tissue development, homeostasis, and cellular signaling. Structurally, HSPG2 consists of five distinct domains: three LDL receptor-like domains, a laminin-like domain, and immunoglobulin repeats, which enable interactions with various ECM components (e.g., collagen, fibronectin) and growth factors (e.g., FGF, VEGF). Its heparan sulfate (HS) chains further mediate ligand binding and regulate signaling pathways involved in angiogenesis, cell adhesion, and wound healing.
Recombinant HSPG2 proteins are engineered to study its biological functions or therapeutic potential. Producing full-length HSPG2 is challenging due to its large size (~470 kDa) and complex post-translational modifications, including glycosylation. Most recombinant versions focus on specific domains or truncated forms, expressed in mammalian systems (e.g., HEK293 cells) to ensure proper folding and sulfation of HS chains. These proteins are vital tools for investigating HSPG2’s role in diseases, such as cancer (where it exhibits dual tumor-promoting or suppressive effects depending on context), cardiovascular disorders, and genetic conditions like Schwartz-Jampel syndrome (caused by *HSPG2* mutations).
In regenerative medicine, recombinant HSPG2 is explored for ECM-mimicking scaffolds to enhance tissue engineering. Its ability to modulate growth factor bioavailability also makes it a candidate for drug delivery systems. Despite technical hurdles in production, recombinant HSPG2 remains a key molecule for deciphering ECM biology and developing targeted therapies.
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