| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HAase |
| Uniprot No | Q9H161 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-411aa |
| 氨基酸序列 | MNAETCVSYCESPAAAMDAYYSPVSQSREGSSPFRAFPGGDKFGTTFLSAAAKAQGFGDAKSRARYGAGQQDLATPLESGAGARGSFNKFQPQPSTPQPQPPPQPQPQQQQPQPQPPAQPHLYLQRGACKTPPDGSLKLQEGSSGHSAALQVPCYAKESSLGEPELPPDSDTVGMDSSYLSVKEAGVKGPQDRASSDLPSPLEKADSESNKGKKRRNRTTFTSYQLEELEKVFQKTHYPDVYAREQLAMRTDLTEARVQVWFQNRRAKWRKRERFGQMQQVRTHFSTAYELPLLTRAENYAQIQNPSWLGNNGAASPVPACVVPCDPVPACMSPHAHPPGSGASSVTDFLSVSGAGSHVGQTHMGSLFGAASLSPGLNGYELNGEPDRKTSSIAALRMKAKEHSAAISWAT |
| 预测分子量 | 44,2 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. |
以下是关于重组HAase(透明质酸酶)的模拟参考文献示例，供参考。建议通过PubMed、Web of Science等学术平台检索最新文献：
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1. **文献名称**: "High-yield expression and characterization of a recombinant human hyaluronidase in Escherichia coli"
**作者**: Zhang L, et al.
**摘要**: 研究报道了在大肠杆菌中高效表达重组人源透明质酸酶(rHuHAase)的优化策略，通过密码子优化和诱导条件调控，获得高纯度酶，并验证其酶活性和稳定性。
2. **文献名称**: "Purification and functional analysis of a novel hyaluronidase from recombinant Pichia pastoris"
**作者**: Smith J, et al.
**摘要**: 利用毕赤酵母系统表达重组HAase，开发了新型纯化工艺，证明其降解透明质酸的高效性，并探讨其在药物递送系统中的潜在应用。
3. **文献名称**: "Structural insights into the catalytic mechanism of recombinant bovine hyaluronidase"
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析重组牛源HAase的三维结构，揭示其底物结合位点及催化机制，为理性设计突变体提供依据。
4. **文献名称**: "Recombinant hyaluronidase enhances tumor permeability for improved chemotherapy delivery"
**作者**: Wang H, et al.
**摘要**: 动物模型中验证重组HAase可有效降解肿瘤基质透明质酸，显著提升化疗药物的肿瘤渗透率和疗效，支持其作为辅助治疗的潜力。
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**注意**：以上为模拟示例，实际文献需通过学术数据库查询。推荐使用关键词“recombinant hyaluronidase”、“HAase expression”或“hyaluronidase application”进行检索。
Hyaluronidase (HAase) is an enzyme that degrades hyaluronic acid (HA), a major component of the extracellular matrix involved in tissue structure, hydration, and cell signaling. Naturally produced in organisms ranging from bacteria to mammals, HAase plays critical roles in physiological and pathological processes, including fertilization, inflammation, and cancer metastasis. The recombinant form of HAase (rHAase) is engineered using biotechnological approaches, typically expressed in microbial (e.g., *E. coli*) or mammalian cell systems (e.g., CHO cells) to ensure high purity, scalability, and reduced immunogenicity compared to animal-derived counterparts.
The development of recombinant HAase addresses limitations of traditional extraction methods, which often yield heterogeneous or contaminated preparations. Recombinant technology allows precise control over enzyme activity, stability, and post-translational modifications. For instance, mammalian-expressed rHAase may retain native glycosylation patterns, enhancing its functional compatibility in therapeutic applications. In contrast, microbial systems offer cost-effective production but may require additional steps to refold denatured proteins.
Clinically, rHAase is utilized to enhance drug diffusion (e.g., improving subcutaneous fluid absorption or local anesthesia spread) and as an adjunct in cancer therapy to increase tumor permeability for chemotherapeutics. In dermatology, it is applied in aesthetic medicine to reverse HA filler overcorrection or improve skin barrier penetration. Research also explores its potential in treating fibrotic diseases and osteoarthritis by modulating HA metabolism.
Ongoing studies focus on optimizing rHAase variants with tailored substrate specificity, pH stability, or prolonged half-life. Safety and regulatory advancements continue to drive its transition from laboratory tools to approved therapeutics, underscoring its versatility in bridging biomedical innovation and clinical needs.
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