| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | METAP1D |
| Uniprot No | Q6UB28 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-335aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSSSPLNHIYLHKQSSSQQRRNFFFRRQRDISHSIVLPAAVSSAHPVPK HIKKPDYVTTGIVPDWGDSIEVKNEDQIQGLHQACQLARHVLLLAGKSLK VDMTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDS RPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDE AIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWH HANDSDLPMEEGMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEH TVLITSRGAQILTKLPHEA |
| 预测分子量 | 37 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METAP1D重组蛋白的3篇参考文献(注：由于METAP1D研究相对较少，部分文献可能涉及相关功能或结构研究，以下为模拟示例)：
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1. **文献名称**：*"Cloning and Characterization of Human METAP1D as a Cytosolic Methionine Aminopeptidase"*
**作者**：Chen X. et al.
**摘要**：本研究成功克隆并表达了人源METAP1D重组蛋白，证实其具有甲硫氨酸氨基肽酶活性，并发现其特异性去除新生蛋白质N端甲硫氨酸的功能对细胞增殖具有调控作用。
2. **文献名称**：*"Structural Insights into METAP1D Substrate Specificity and Inhibition"*
**作者**：Wang L. et al.
**摘要**：通过X射线晶体学解析了METAP1D重组蛋白的三维结构，揭示了其底物结合口袋的独特构象，并筛选出小分子抑制剂，为靶向METAP1D的抗癌药物开发提供理论基础。
3. **文献名称**：*"METAP1D Deficiency Alters Angiogenesis via Dysregulation of Mitochondrial Proteins"*
**作者**：Kim J. et al.
**摘要**：利用重组METAP1D蛋白进行功能实验，发现其通过调控线粒体相关蛋白的加工影响血管生成，提示METAP1D在缺血性疾病中的潜在治疗价值。
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**注**：以上文献为示例，实际研究中建议通过PubMed或Web of Science以“METAP1D recombinant”“methionine aminopeptidase 1D”等关键词检索最新论文。如需具体文献，可提供更详细的研究方向以便进一步筛选。
**Background of METAP1D Recombinant Protein**
Methionine aminopeptidase 1D (METAP1D), also known as METAP2 or MAP1D, is a member of the methionine aminopeptidase family, which plays a critical role in post-translational protein modification. METAP enzymes catalyze the removal of initiator methionine residues from nascent polypeptides, a process essential for protein maturation, stability, and functional diversity. Unlike its isoform METAP1. METAP1D exhibits distinct substrate specificity and regulatory mechanisms, contributing to its unique biological roles.
Recombinant METAP1D is engineered for research and therapeutic applications, often produced in heterologous expression systems like *E. coli* or mammalian cells. Its recombinant form retains enzymatic activity, enabling studies on its structure, catalytic mechanism, and interaction with inhibitors. METAP1D is implicated in angiogenesis, cell proliferation, and tumorigenesis, with elevated expression observed in certain cancers. This has spurred interest in developing METAP1D-targeted therapies, particularly for cancer treatment.
Structurally, METAP1D contains a conserved catalytic domain with a dinuclear metal center (typically cobalt or manganese) critical for its enzymatic function. Research highlights its role in modulating the N-terminal processing of proteins involved in signal transduction and metabolic pathways. Dysregulation of METAP1D has been linked to pathological conditions, including cardiovascular diseases and metabolic disorders, underscoring its therapeutic potential.
Current studies focus on characterizing recombinant METAP1D’s biochemical properties, inhibitor screening, and elucidating its role in disease mechanisms. Its recombinant availability accelerates drug discovery and functional genomics, positioning METAP1D as a promising target for precision medicine.
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