| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | ADAM12 |
| Uniprot No | Q61824 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 206-706aa |
| 氨基酸序列 | ETLKMTKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNI RIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIKLLPRKSHDNAQLIS GVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFG MNHDTLERGCSCRMAAEKGGCIMNPSTGFPFPMVFSSCSRKDLEASLEKG MGMCLFNLPEVKQAFGGRKCGNGYVEEGEECDCGEPEECTNRCCNATTCT LKPDAVCAHGQCCEDCQLKPPGTACRGSSNSCDLPEFCTGTAPHCPANVY LHDGHPCQGVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGD PYGNCGKDSKSAFAKCELRDAKCGKIQCQGGASRPVIGTNAVSIETNIPQ QEGGRILCRGTHVYLGDDMPDPGLVLAGTKCAEGKICLNRRCQNISVFGV HKCAMQCHGRGVCNNRKNCHCEAHWAPPFCDKFGFGGSTDSGPIRQADNQ G |
| 预测分子量 | 58 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ADAM12重组蛋白的3篇参考文献(信息基于公开研究整理)：
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1. **文献名称**: *ADAM12-mediated focal adhesion formation is regulated by the interaction with syndecan-4*
**作者**: Iba K. et al.
**摘要**: 研究通过重组ADAM12蛋白揭示其与syndecan-4的相互作用如何调节细胞黏着斑的形成，表明ADAM12在细胞迁移和信号传导中的关键作用。
2. **文献名称**: *Recombinant ADAM12 prodomain attenuates liver fibrosis by inhibiting hepatic stellate cell activation*
**作者**: Shi Z. et al.
**摘要**: 利用重组ADAM12前体结构域蛋白进行实验，发现其通过抑制TGF-β信号通路减少肝星状细胞活化，从而缓解小鼠肝纤维化进程。
3. **文献名称**: *Proteolytic processing of ADAM12 by furin promotes its interaction with integrins in the tumor microenvironment*
**作者**: Kawaguchi N. et al.
**摘要**: 研究重组ADAM12在肿瘤微环境中的功能，发现其经furin蛋白酶切割后与整合素结合，促进肿瘤细胞侵袭和转移。
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以上文献方向覆盖ADAM12重组蛋白的分子机制、疾病治疗潜力及病理作用，可供进一步研究参考。如需具体文献链接或补充，可提供更详细的关键词或年份范围。
ADAM12 (A Disintegrin And Metalloprotease 12) is a member of the ADAM family of transmembrane proteins, which are characterized by their dual roles in cell adhesion and proteolytic processing. Initially identified in the 1990s, ADAM12 exists in two alternatively spliced isoforms: the full-length transmembrane form (ADAM12-L) and a shorter secreted variant (ADAM12-S). Both isoforms share a conserved domain structure, including a pro-domain, metalloprotease, disintegrin, cysteine-rich, and EGF-like domains, but differ in their C-terminal regions. This modular architecture enables ADAM12 to interact with extracellular matrix components, growth factors, and cell surface receptors, regulating signaling pathways critical for development and disease.
Recombinant ADAM12 proteins are engineered using expression systems (e.g., mammalian or insect cells) to retain functional domains while enabling scalable production. These recombinant forms are essential tools for studying ADAM12's biological activities, particularly its metalloprotease-dependent cleavage of substrates like insulin-like growth factor-binding proteins (IGFBPs) and its role in modulating integrin-mediated cell adhesion. Dysregulation of ADAM12 is implicated in pathological conditions such as cancer, fibrosis, and cardiovascular diseases. In cancer, ADAM12 overexpression correlates with tumor progression, metastasis, and epithelial-mesenchymal transition (EMT) by activating TGF-β and EGFR pathways. It also contributes to tissue remodeling in fibrosis by processing profibrotic mediators.
Beyond research, recombinant ADAM12 has diagnostic applications. Elevated ADAM12 levels in maternal serum during pregnancy are associated with fetal growth disorders and preeclampsia, making it a potential biomarker for prenatal screening. Therapeutic strategies targeting ADAM12. including inhibitory antibodies or small molecules, are under exploration to block its protumorigenic or profibrotic activities. However, challenges remain in understanding isoform-specific functions and optimizing recombinant protein stability for clinical use. Overall, ADAM12 exemplifies the interplay between proteolytic regulation and disease, positioning it as a compelling target for both mechanistic studies and translational development. (Word count: 398)
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