纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | HAPLN1 |
Uniprot No | P10915 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 16-354aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSDHLSDNYTLDHDRAIHIQAENGPHLLV EAEQAKVFSHRGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDYLKEV DVFVSMGYHKKTYGGYQGRVFLKGGSDSDASLVITDLTLEDYGRYKCEVI EGLEDDTVVVALDLQGVVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFD QLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNYGFWD KDKSRYDVFCFTSNFNGRFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQI FAAWKILGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVGFPDKKH KLYGVYCFRAYN |
预测分子量 | 41 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. **"HAPLN1 potentiates the chondrogenic differentiation of human mesenchymal stem cells"**
- **作者**: Smith A, et al.
- **摘要**: 研究探讨了重组HAPLN1蛋白通过调控细胞外基质稳定性促进人间充质干细胞向软骨细胞分化的机制,表明其在软骨组织工程中的潜在应用价值。
2. **"Recombinant HAPLN1 inhibits tumor invasion by modulating hyaluronan-rich matrix remodeling"**
- **作者**: Chen L, et al.
- **摘要**: 发现重组HAPLN1通过稳定透明质酸-蛋白聚糖复合物,抑制肿瘤细胞侵袭和转移,提示其在癌症治疗中的潜在作用。
3. **"HAPLN1 enhances the mechanical properties of engineered cartilage constructs"**
- **作者**: Park JH, et al.
- **摘要**: 研究证明重组HAPLN1蛋白可显著提高工程化软骨的机械强度和弹性,为关节修复生物材料开发提供了新策略。
4. **"Role of HAPLN1 in maintaining vascular integrity through extracellular matrix stabilization"**
- **作者**: Gupta R, et al.
- **摘要**: 揭示了重组HAPLN1通过调节血管周围基质结构,改善内皮屏障功能,可能对血管相关疾病具有治疗意义。
(注:以上文献为示例,实际引用需根据具体研究内容检索真实文献。)
Hyaluronan and proteoglycan link protein 1 (HAPLN1), also known as cartilage link protein 1 (CRTL1), is a key extracellular matrix (ECM) component that stabilizes interactions between hyaluronan (HA) and proteoglycans such as aggrecan. This glycoprotein plays a critical role in maintaining the structural integrity and hydration of tissues, particularly in cartilage, the vitreous humor of the eye, and other HA-rich environments. By binding to both HA and aggrecan, HAPLN1 facilitates the formation of high-molecular-weight complexes that confer mechanical resilience, shock absorption, and elasticity to tissues. Its presence is essential for normal joint function, as it prevents HA degradation and ensures ECM stability under physiological stress.
Structurally, HAPLN1 contains two conserved domains: an N-terminal HA-binding region and a C-terminal link module shared with other proteoglycan-associated proteins. These domains enable its dual role in crosslinking HA and stabilizing proteoglycan networks. Dysregulation of HAPLN1 has been implicated in degenerative conditions like osteoarthritis, where reduced expression correlates with cartilage erosion and ECM breakdown. Conversely, its overexpression is observed in certain cancers, suggesting a role in tumor microenvironment modulation.
Recombinant HAPLN1 is produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications, such as disulfide bonding, which are critical for its biological activity. It serves as a vital tool for studying ECM dynamics, tissue engineering, and disease mechanisms. In regenerative medicine, recombinant HAPLN1 is explored for enhancing scaffold-based cartilage repair or modulating HA-dependent cellular behaviors in 3D culture models. Its therapeutic potential is also being investigated for restoring ECM homeostasis in joint diseases or counteracting pathological ECM remodeling in cancer metastasis.
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