| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CPM |
| Uniprot No | P14384 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-423aa |
| 氨基酸序列 | LDF NYHRQEGMEA FLKTVAQNYS SVTHLHSIGK SVKGRNLWVL VVGRFPKEHR IGIPEFKYVA NMHGDETVGR ELLLHLIDYL VTSDGKDPEI TNLINSTRIH IMPSMNPDGF EAVKKPDCYY SIGRENYNQY DLNRNFPDAF EYNNVSRQPE TVAVMKWLKT ETFVLSANLH GGALVASYPF DNGVQATGAL YSRSLTPDDD VFQYLAHTYA SRNPNMKKGD ECKNKMNFPN GVTNGYSWYP LQGGMQDYNY IWAQCFEITL ELSCCKYPRE EKLPSFWNNN KASLIEYIKQ VHLGVKGQVF DQNGNPLPNV IVEVQDRKHI CPYRTNKYGE YYLLLLPGSY IINVTVPGHD PHITKVIIPE KSQNFSALKK DILLPFQGQL DSIPVSNPSC PMIPLYRNLP DHS |
| 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. |
以下是关于CPM(羧肽酶M)重组蛋白研究的模拟参考文献示例，供参考：
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1. **标题**: "Expression and Characterization of Recombinant Human Carboxypeptidase M in Mammalian Cells"
**作者**: Zhang, L. et al.
**摘要**: 本研究在HEK293细胞中成功表达并纯化了重组人CPM蛋白，通过酶动力学分析证实其具有底物特异性，能够水解缓激肽和E选择素配体，揭示了其在炎症反应中的潜在调控作用。
2. **标题**: "Functional Analysis of CPM Mutants Expressed in Insect Cells Using Baculovirus System"
**作者**: Tanaka, K. & Yamamoto, S.
**摘要**: 利用杆状病毒-昆虫细胞系统表达CPM重组蛋白及突变体，发现特定结构域(如跨膜区缺失)显著影响其膜结合能力和酶活性，为CPM功能域研究提供实验依据。
3. **标题**: "Crystal Structure of Recombinant CPM Reveals Substrate-Binding Mechanism"
**作者**: Müller, R. et al.
**摘要**: 通过X射线晶体学解析重组CPM的3D结构，阐明其活性位点与底物结合的分子机制，为开发靶向CPM的抑制剂奠定结构基础。
4. **标题**: "Role of Recombinant CPM in Cancer Cell Migration: In Vitro and In Vivo Models"
**作者**: Chen, H. & Wang, Q.
**摘要**: 在肿瘤细胞中过表达重组CPM，发现其通过调节细胞外基质肽的水解促进癌细胞迁移，提示CPM可能成为抗肿瘤治疗的潜在靶点。
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注：以上为模拟文献，实际研究需通过学术数据库(如PubMed、Web of Science)检索关键词 **"recombinant carboxypeptidase M"** 或 **"CPM protein expression"** 获取真实文献。
**Background of CPM Recombinant Protein**
Carboxypeptidase M (CPM), a glycosylphosphatidylinositol (GPI)-anchored membrane protein, belongs to the M14 family of metallocarboxypeptidases. It catalyzes the cleavage of C-terminal basic residues from bioactive peptides, regulating processes like inflammation, hormone processing, and cell signaling. Initially identified in human placental membranes, CPM is expressed in various tissues, including the kidneys, lungs, and immune cells, underscoring its role in homeostasis and disease.
Recombinant CPM protein is produced using genetic engineering techniques, often via expression systems like mammalian cells (e.g., CHO or HEK293) to ensure proper post-translational modifications. This engineered protein retains enzymatic activity, enabling researchers to study its substrate specificity, inhibition mechanisms, and interaction with physiological pathways. CPM’s ability to modulate peptides such as bradykinin, osteopontin, and complement components links it to conditions like fibrosis, cancer progression, and autoimmune disorders. For instance, elevated CPM levels correlate with tumor invasiveness, suggesting its potential as a therapeutic target or biomarker.
The development of recombinant CPM has advanced drug discovery, particularly in designing inhibitors to curb its pro-disease activities. Additionally, it serves as a tool for structural studies, elucidating substrate-binding sites and catalytic domains through X-ray crystallography. Its soluble form (lacking the GPI anchor) is widely used in *in vitro* assays due to ease of handling and consistent activity.
Overall, CPM recombinant protein bridges basic research and clinical applications, offering insights into peptidase biology and paving the way for novel diagnostics or therapies targeting CPM-associated diseases.
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