| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HABP2 |
| Uniprot No | Q14520 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 314-560aa |
| 氨基酸序列 | IYGGFKSTAGKHPWQASLQSSLPLTISMPQGHFCGGALIHPCWVLTAAHCTDIKTRHLKVVLGDQDLKKEEFHEQSFRVEKIFKYSHYNERDEIPHNDIALLKLKPVDGHCALESKYVKTVCLPDGSFPSGSECHISGWGVTETGKGSRQLLDAKVKLIANTLCNSRQLYDHMIDDSMICAGNLQKPGQDTCQGDSGGPLTCEKDGTYYVYGIVSWGLECGKRPGVYTQVTKFLNWIKATIKSESGF |
| 预测分子量 | 43.3kDa |
| 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HABP2重组蛋白的参考文献及其摘要概括：
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1. **文献名称**：*"Functional characterization of the HABP2 p.G534E variant in papillary thyroid carcinoma"*
**作者**：Goudarzi, H. M., et al.
**摘要**：该研究通过重组HABP2蛋白实验，证实p.G534E突变导致其丝氨酸蛋白酶活性丧失，并降低甲状腺癌细胞侵袭能力，提示HABP2可能作为抑癌基因发挥作用。
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2. **文献名称**：*"Recombinant HABP2 binds hyaluronan and modulates cell adhesion in vitro"*
**作者**：Zhang, Y., & Wang, L.
**摘要**：研究利用大肠杆菌表达系统制备重组HABP2蛋白，发现其通过结合透明质酸调控细胞外基质黏附，并在划痕实验中抑制上皮细胞迁移，提示其在组织修复中的潜在应用。
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3. **文献名称**：*"Structural insights into the hyaluronan-binding domain of HABP2 through recombinant protein crystallization"*
**作者**：Smith, J. R., et al.
**摘要**：通过重组HABP2的晶体结构解析，揭示其C端结构域中关键氨基酸残基与透明质酸的特异性结合模式，为开发靶向HABP2的抑制剂提供结构基础。
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(注：以上文献为虚拟示例，实际引用需根据具体研究补充真实文献信息。)
**Background of HABP2 Recombinant Protein**
HABP2 (Hyaluronan Binding Protein 2), also known as serine protease 3 or TIA-2. is a multifunctional protein encoded by the *HABP2* gene. It belongs to the serine protease family and plays roles in extracellular matrix remodeling, coagulation, and cell signaling. Structurally, HABP2 contains an N-terminal hyaluronan-binding domain and a C-terminal catalytic domain with trypsin-like protease activity. Its ability to bind hyaluronan, a major component of the extracellular matrix, links it to processes like cell adhesion, migration, and tissue repair.
HABP2 gained attention due to its dual role in both physiological and pathological contexts. In normal physiology, it regulates fibrinolysis by activating plasminogen and interacts with coagulation factors (e.g., Factor VII). However, dysregulation of HABP2 has been implicated in cancer progression, particularly in thyroid, breast, and liver cancers, where it may promote tumor invasion and metastasis. A germline mutation (G534E) in *HABP2* was controversially associated with familial non-medullary thyroid cancer, though its pathogenic role remains under investigation.
Recombinant HABP2 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) for functional studies. Its purified form enables researchers to explore enzymatic activity, ligand interactions, and signaling pathways in vitro. Additionally, HABP2 serves as a potential biomarker or therapeutic target in diseases involving abnormal coagulation or matrix remodeling. Challenges in its study include post-translational modifications affecting activity and the need for precise structural characterization. Current research focuses on clarifying its tissue-specific roles and validating its clinical relevance in oncology and vascular biology.
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