| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EMILIN2 |
| Uniprot No | Q9BXX0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1053aa |
| 氨基酸序列 | MWQPRRPWPRVPWRWALALLALVGAGLCHAGPQPGYPARPSARNKNWCAYIVNKNVSCSVLEGSESFIQAQYNCAWNQMPCPSALVYRVNFRPRYVTRYKTVTQLEWRCCPGFRGGDCQEGPKDPVKTLRPTPARPRNSLKKATDNEPSQFSEPRKTLSPTGTAQPSWGVDPKEGPQELQEKKIQVLEEKVLRLTRTVLDLQSSLAGVSENLKHATQDDASRTRAPGLSSQHPKPDTTVSGDTETGQSPGVFNTKESGMKDIKSELAEVKDTLKNKSDKLEELDGKVKGYEGQLRQLQEAAQGPTVTMTTNELYQAYVDSKIDALREELMEGMDRKLADLKNSCEYKLTGLQQQCDDYGSSYLGVIELIGEKETSLRKEINNLRARLQEPSAQANCCDSEKNGDIGQQIKTLDQKIERVAEATRMLNGRLDNEFDRLIVPEPDVDFDAKWNELDARINVTEKNAEEHCFYIEETLRGAINGEVGDLKQLVDQKIQSLEDRLGSVLLQMTNNTGAELSPPGAAALPGVSGSGDERVMMELNHLKDKVQVVEDICLLNIQGKPHGMEGALPNREDRAVRDSLHLLKSLNDTMHRKFQETEQTIQKLQQDFSFLYSQLNHTENDVTHLQKEMSNCRAGENAGMGRFTKVGEQERTVDTLPSPQHPVAHCCSQLEERWQRLQSQVISELDACKECTQGVQREVSMVEGRVSHMEKTCSKLDSISGNLQRIKEGLNKHVSSLWNCVRQMNGTLRSHSRDISGLKNSVQQFYSHVFQISTDLQDLVKFQPSAKAPSPPPPAEAPKEPLQPEPAPPRPSGPATAEDPGRRPVLPQRPPEERPPQPPGSTGVIAETGQAGPPAGAGVSGRGLPRGVDGQTGSGTVPGAEGFAGAPGYPKSPPVASPGAPVPSLVSFSAGLTQKPFPSDGGVVLFNKVLVNDGDVYNPSTGVFTAPYDGRYLITATLTPERDAYVEAVLSVSNASVAQLHTAGYRREFLEYHRPPGALHTCGGPGAFHLIVHLKAGDAVNVVVTGGKLAHTDFDEMYSTFSGVFLYPFLSHL |
| 预测分子量 | 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3篇关于EMILIN2重组蛋白的参考文献及其核心内容概括：
1. **文献名称**: "EMILIN2 regulates extracellular matrix remodeling and promotes mesenchymal transition in glioblastoma"
**作者**: Spessotto P, et al.
**摘要**: 研究利用重组EMILIN2蛋白揭示了其在胶质母细胞瘤微环境中的作用，发现其通过调控细胞外基质重塑和激活整合素信号通路，促进肿瘤细胞的间充质转化及侵袭能力。
2. **文献名称**: "Structural and functional characterization of the EMILIN2 gC1q domain in angiogenesis"
**作者**: Danussi C, et al.
**摘要**: 通过重组表达EMILIN2的gC1q结构域，发现该区域能够特异性结合内皮细胞表面受体，抑制血管生成，并阐明了其在抑制肿瘤血管形成中的潜在治疗价值。
3. **文献名称**: "Recombinant EMILIN2 suppresses breast cancer metastasis by modulating TGF-β signaling"
**作者**: Colombatti A, et al.
**摘要**: 研究证明重组EMILIN2蛋白通过阻断TGF-β/Smad信号通路，抑制乳腺癌细胞的迁移和转移，提示其作为转移抑制因子的新机制。
**备注**：以上文献为示例性内容，实际文献需通过PubMed/Google Scholar检索确认。EMILIN2研究多集中于细胞外基质调控、肿瘤转移及血管生成领域，建议结合具体研究方向筛选文献。
**Background of EMILIN2 Recombinant Protein**
EMILIN2 (Elastin Microfibril Interface Located Protein 2) is a glycoprotein belonging to the EMILIN family, which includes extracellular matrix (ECM) proteins involved in tissue organization, cell adhesion, and signaling. Structurally, EMILIN2 contains characteristic domains such as a C1q globular domain at the C-terminus, a coiled-coil region, and an N-terminal cysteine-rich EMI domain. These domains enable interactions with other ECM components (e.g., elastin, fibulin, integrins) and cell surface receptors, influencing ECM assembly and cellular behavior.
EMILIN2 is expressed in various tissues, including blood vessels, skin, and developing organs, where it contributes to elastic fiber formation and tissue elasticity. Studies suggest its role in modulating TGF-β signaling, a pathway critical for cell proliferation, differentiation, and fibrosis. Dysregulation of EMILIN2 has been linked to pathological conditions such as cardiovascular disorders, cancer metastasis, and fibrotic diseases. For instance, EMILIN2 deficiency in mice results in vascular abnormalities, highlighting its importance in vascular development.
Recombinant EMILIN2 protein is typically produced using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications. It is purified via affinity chromatography and validated for functionality in assays examining cell adhesion, migration, or ECM remodeling. Researchers utilize EMILIN2 recombinant protein to study its mechanistic roles in tissue homeostasis, disease models, and regenerative therapies. Its potential as a therapeutic target or biomaterial in tissue engineering underscores its relevance in biomedical research. Ongoing studies aim to clarify its interactions with signaling molecules and ECM networks, offering insights into novel diagnostic or therapeutic strategies.
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