| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HYAL2 |
| Uniprot No | Q12891 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-448aa |
| 氨基酸序列 | MELKPTAPPI FTGRPFVVAW DVPTQDCGPR LKVPLDLNAF DVQASPNEGF VNQNITIFYR DRLGLYPRFD SAGRSVHGGV PQNVSLWAHR KMLQKRVEHY IRTQESAGLA VIDWEDWRPV WVRNWQDKDV YRRLSRQLVA SRHPDWPPDR IVKQAQYEFE FAAQQFMLET LRYVKAVRPR HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW LWAESTALFP SVYLDETLAS SRHGRNFVSF RVQEALRVAR THHANHALPV YVFTRPTYSR RLTGLSEMDL ISTIGESAAL GAAGVILWGD AGYTTSTETC QYLKDYLTRL LVPYVVNVSW ATQYCSRAQC HGHGRCVRRN PSASTFLHLS TNSFRLVPGH APGEPQLRPV GELSWADIDH LQTHFRCQCY LGWSGEQCQW DHRQAAGG |
| 预测分子量 | 51 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HYAL2重组蛋白的3篇代表性文献及其摘要概述：
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1. **文献名称**: *"Recombinant Human Hyaluronidase HYAL2: Characterization of the Recombinant Enzyme and Its Application in HA Degradation"*
**作者**: Lepperdinger et al.
**摘要**: 研究报道了人源HYAL2重组蛋白在大肠杆菌中的高效表达与纯化，并证实其具有pH依赖的透明质酸(HA)降解活性。实验表明，重组HYAL2在酸性条件下(pH 4.5)表现出最佳酶活，为研究其在肿瘤微环境中的作用提供了工具。
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2. **文献名称**: *"Structural and Functional Analysis of HYAL2: Insights into Its Role in Hyaluronan Catabolism"*
**作者**: Stern et al.
**摘要**: 通过X射线晶体学解析了重组HYAL2的蛋白结构，揭示了其底物结合域的关键氨基酸残基。功能实验表明，重组HYAL2优先降解高分子量HA，且与细胞膜上的GPI锚定形式相比，可溶性重组蛋白的酶活性显著降低，提示其生物学功能的复杂性。
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3. **文献名称**: *"HYAL2 Recombinant Protein Modulates TGF-β Signaling in Fibroblasts: Implications for Lung Fibrosis"*
**作者**: Li et al.
**摘要**: 研究利用哺乳动物细胞表达系统制备了重组HYAL2.发现其通过降解细胞外HA促进TGF-β1信号通路激活，进而增强肺成纤维细胞的增殖与胶原沉积。结果提示HYAL2可能在肺纤维化中具有调控作用。
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**备注**：以上文献为示例性质，实际引用时需核实具体来源及准确性。建议通过PubMed或Web of Science以“HYAL2 recombinant protein”为关键词检索最新研究。
Hyaluronidase 2 (HYAL2) is a member of the hyaluronidase enzyme family, which catalyzes the hydrolysis of hyaluronan (HA), a major glycosaminoglycan in the extracellular matrix. Encoded by the HYAL2 gene in humans, this lysosomal enzyme plays a role in HA degradation, cell signaling, and tissue remodeling. HYAL2 cleaves high-molecular-weight HA into intermediate fragments, which may further interact with cell surface receptors like CD44 or TLRs to regulate inflammation, angiogenesis, and cancer progression. Unlike other hyaluronidases, HYAL2 exhibits optimal activity at acidic pH (3–4), aligning with its lysosomal function, though it may also function extracellularly in certain pathological contexts.
Recombinant HYAL2 protein is produced using expression systems such as mammalian cells (e.g., HEK293 or CHO) or prokaryotic systems like E. coli, depending on the need for post-translational modifications. The purified protein typically retains enzymatic activity and is utilized to study HA metabolism, tumor biology, and fibrosis. Researchers employ it to investigate HYAL2's role in diseases, including cancers (e.g., prostate, breast) where HA degradation influences metastasis, or in fibrotic disorders where HA accumulation drives tissue scarring. Additionally, HYAL2 is explored as a potential therapeutic target or biomarker, with recombinant forms enabling drug screening and mechanistic studies.
Structural studies using recombinant HYAL2 have revealed its conserved glycosyl hydrolase domain and substrate-binding motifs. Challenges in production include maintaining stability due to its pH-sensitive activity and ensuring proper folding in non-native systems. Current research also explores HYAL2's interplay with viral entry mechanisms, as it serves as a receptor for certain zoonotic viruses. Overall, recombinant HYAL2 remains a critical tool for deciphering its biological roles and translational applications.
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