| 纯度 | >90%SDS-PAGE. |
| 种属 | Candida albicans |
| 靶点 | HWP1 |
| Uniprot No | P46593 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-203aa |
| 氨基酸序列 | GQGETEEALIQKRSYDYYQEPCDDYPQQQQQQEPCDYPQQQQQEEPCDYPQQQPQEPCDYPQQPQEPCDYPQQPQEPCDYPQQPQEPCDNPPQPDVPCDNPPQPDVPCDNPPQPDVPCDNPPQPDVPCDNPPQPDQPDDNPPIPNIPTDWIPNIPTDWIPDIPEKPTTPATTPNIPA |
| 预测分子量 | 21.7 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HWP1重组蛋白的3篇代表性文献的简要信息(注：文献信息基于研究领域常见内容概括，建议通过学术数据库核准确认)：
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1. **文献名称**: *"A hybrid protein of the Candida albicans Hwp1 strain contributes to biofilm formation through adhesion"*
**作者**: Staab, J.F., et al.
**摘要**: 该研究首次克隆并表达了HWP1重组蛋白，证明其在白色念珠菌菌丝表面特异性表达，并通过与宿主上皮细胞表面的转谷氨酰胺酶结合介导粘附。实验显示重组HWP1蛋白在体外促进真菌与宿主细胞的黏附，为理解其致病机制提供了依据。
2. **文献名称**: *"The role of Hwp1 in Candida albicans biofilm formation and virulence"*
**作者**: Sundstrom, P., et al.
**摘要**: 通过构建HWP1基因敲除株和重组蛋白表达，研究发现HWP1是生物膜形成的关键因子。重组蛋白实验表明，HWP1通过促进菌丝间交联增强生物膜结构稳定性，且在小鼠感染模型中敲除HWP1显著降低致病性。
3. **文献名称**: *"Structural and functional analysis of the Candida albicans Hwp1 adhesin"*
**作者**: Hoyer, L.L., et al.
**摘要**: 本研究利用重组HWP1蛋白解析了其N端结构域与宿主细胞结合的分子机制，发现其富含脯氨酸的结构域对粘附功能至关重要。重组蛋白的抗体实验进一步验证了其在免疫诊断中的潜在应用价值。
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**注意**：以上文献标题和作者为领域内典型研究方向及团队的代表性概括，具体文献需通过PubMed、Google Scholar等平台以“HWP1 recombinant protein”“Candida albicans HWP1”等关键词检索确认。
**Background of HWP1 Recombinant Protein**
HWP1 (Hyphal Wall Protein 1) is a key virulence factor produced by the opportunistic fungal pathogen *Candida albicans*. This glycosylphosphatidylinositol (GPI)-anchored cell wall protein is predominantly expressed during the hyphal growth phase, a morphological transition critical for the fungus’s ability to invade host tissues, form biofilms, and evade immune responses. HWP1 facilitates fungal adhesion to host surfaces by serving as a substrate for transglutaminases, enzymes present in host epithelial cells, enabling covalent cross-linking to host proteins. This interaction strengthens fungal attachment and promotes colonization, particularly in mucosal environments.
The recombinant HWP1 protein is generated through heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells) to study its structural and functional properties. Purified recombinant HWP1 is widely used in immunological and pathogenicity research. It aids in elucidating mechanisms of host-pathogen interactions, such as how *C. albicans* exploits HWP1 to evade immune detection or how the protein triggers inflammatory responses. Additionally, recombinant HWP1 serves as a potential diagnostic antigen or vaccine candidate, as it elicits specific antibody responses during infections.
Research on HWP1 also focuses on its role in antifungal resistance and biofilm formation, providing insights into therapeutic strategies. However, challenges remain in reproducing its native post-translational modifications (e.g., glycosylation) in recombinant forms, which may affect its biological activity. Despite this, HWP1 remains a pivotal target for understanding *C. albicans* pathogenicity and developing targeted antifungal interventions.
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