| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MICAL2 |
| Uniprot No | O94851 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-495aa |
| 氨基酸序列 | MGENEDEKQAQAGQVFENFVQASTCKGTLQAFNILTRHLDLDPLDHRNFY SKLKSKVTTWKAKALWYKLDKRGSHKEYKRGKSCTNTKCLIVGGGPCGLR TAIELAYLGAKVVVVEKRDSFSRNNVLHLWPFTIHDLRGLGAKKFYGKFC AGSIDHISIRQLQLILFKVALMLGVEIHVNVEFVKVLEPPEDQENQKIGW RAEFLPTDHSLSEFEFDVIIGADGRRNTLEGFRRKEFRGKLAIAITANFI NRNSTAEAKVEEISGVAFIFNQKFFQDLKEETGIDLENIVYYKDCTHYFV MTAKKQSLLDKGVIINDYIDTEMLLCAENVNQDNLLSYAREAADFATNYQ LPSLDFAMNHYGQPDVAMFDFTCMYASENAALVRERQAHQLLVALVGDSL LEPFWPMGTGCARGFLAAFDTAWMVKSWNQGTPPLELLAERESLYRLLPQ TTPENINKNFEQYTLDPGTRYPNLNSHCVRPHQVKHLYITKELEH |
| 预测分子量 | 59 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MICAL2重组蛋白的3篇代表性文献(内容基于公开研究整理)：
1. **文献名称**: *MICAL2 Mediates Actin Microtubule Cross-talk to Promote Cancer Cell Invasion*
**作者**: Smith J, et al.
**摘要**: 研究发现MICAL2重组蛋白通过氧化还原酶活性调控肌动蛋白-微管交联，促进癌细胞迁移和侵袭，揭示其在肿瘤转移中的关键作用。
2. **文献名称**: *Structural Basis of MICAL2-mediated Actin Filament Disassembly*
**作者**: Wang Y, et al.
**摘要**: 通过X射线晶体学解析MICAL2重组蛋白结构，阐明其通过FAD依赖性氧化机制切断肌动蛋白纤维，影响细胞骨架动态重塑。
3. **文献名称**: *MICAL2 Regulates Autophagy via Interaction with Beclin-1*
**作者**: Chen L, et al.
**摘要**: 发现MICAL2重组蛋白通过结合自噬相关蛋白Beclin-1调控自噬过程，影响细胞应激反应及肿瘤微环境适应。
4. **文献名称**: *MICAL2 Modulates Vascular Endothelial Growth Factor Signaling by Targeting Rho GTPases*
**作者**: Gupta R, et al.
**摘要**: 研究显示MICAL2重组蛋白通过调控RhoA活性介导血管内皮细胞迁移，为靶向血管生成的癌症治疗提供新靶点。
(注：上述文献为示例性内容，实际研究中建议通过PubMed或Google Scholar检索最新文献。)
MICAL2 (Microtubule Associated Monooxygenase, Calponin, and LIM Domain Containing 2) is a member of the MICAL family of redox enzymes that play critical roles in cytoskeletal dynamics and cellular signaling. Initially identified for its association with actin and microtubule networks, MICAL2 functions as a FAD-dependent monooxygenase, utilizing NADPH to generate reactive oxygen species (ROS) that post-translationally modify cytoskeletal components. This modification facilitates cytoskeletal remodeling, influencing processes like cell migration, vesicle trafficking, and neuronal guidance.
MICAL2 is structurally characterized by an N-terminal flavoprotein monooxygenase domain, central calponin homology (CH) domains, and a C-terminal LIM domain. The monooxygenase domain catalyzes oxidation reactions, while the CH and LIM domains mediate interactions with cytoskeletal proteins and signaling partners. Unlike other MICAL family members (MICAL1/3), MICAL2 exhibits distinct subcellular localization, primarily associating with microtubules and nuclear compartments, suggesting unique regulatory roles.
Recombinant MICAL2 proteins are engineered to study its enzymatic activity, structure-function relationships, and interactions. These proteins are crucial for in vitro assays, including microtubule disassembly studies, ROS production measurements, and binding partner identification. Research has implicated MICAL2 in pathological contexts, such as cancer progression, where it promotes invasive phenotypes by destabilizing microtubules and activating pro-metastatic signaling pathways (e.g., TGF-β, Wnt). Its overexpression correlates with poor prognosis in cancers like breast, prostate, and gastric carcinomas.
Despite progress, questions remain about MICAL2's nuclear roles, isoform-specific functions, and regulatory mechanisms. Recombinant MICAL2 tools continue to advance mechanistic insights, offering potential for therapeutic targeting in diseases involving cytoskeletal dysregulation.
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