纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | METAP1 |
Uniprot No | P53582 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-386aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAAVETR VCETDGCSSE AKLQCPTCIK LGIQGSYFCS QECFKGSWAT HKLLHKKAKD EKAKREVSSW TVEGDINTDP WAGYRYTGKL RPHYPLMPTR PVPSYIQRPD YADHPLGMSE SEQALKGTSQ IKLLSSEDIE GMRLVCRLAR EVLDVAAGMI KPGVTTEEID HAVHLACIAR NCYPSPLNYY NFPKSCCTSV NEVICHGIPD RRPLQEGDIV NVDITLYRNG YHGDLNETFF VGEVDDGARK LVQTTYECLM QAIDAVKPGV RYRELGNIIQ KHAQANGFSV VRSYCGHGIH KLFHTAPNVP HYAKNKAVGV MKSGHVFTIE PMICEGGWQD ETWPDGWTAV TRDGKRSAQF EHTLLVTDTG CEILTRRLDS ARPHFMSQF |
预测分子量 | 46 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. |
以下是与METAP1重组蛋白相关的3篇代表性文献摘要:
1. **文献名称**: "Crystal Structure of Human Methionine Aminopeptidase-1 Complexed with Fumagillin"
**作者**: Liu S, et al.
**摘要**: 报道人源METAP1重组蛋白的晶体结构,阐明其与抑制剂Fumagillin的结合模式,揭示酶活性位点的关键氨基酸残基,为靶向药物设计提供结构基础。
2. **文献名称**: "Expression and Characterization of Recombinant Methionine Aminopeptidase from *Plasmodium falciparum*"
**作者**: Kumar R, et al.
**摘要**: 描述恶性疟原虫METAP1在大肠杆菌中的重组表达与纯化,验证其甲硫氨酸切除活性,并证明其作为抗疟药物开发靶点的潜力。
3. **文献名称**: "Functional Analysis of METAP1 in Angiogenesis Using Recombinant Protein Knockdown Models"
**作者**: Chen J, et al.
**摘要**: 通过重组METAP1蛋白与siRNA联用实验,证明METAP1通过调节eIF2α磷酸化影响内皮细胞增殖,提示其在血管生成中的调控作用。
(注:以上内容为基于领域知识的模拟文献,实际引用请通过PubMed/Google Scholar检索最新研究)
**Background of METAP1 Recombinant Protein**
Methionine aminopeptidase 1 (METAP1) is a conserved metalloenzyme critical for post-translational protein modification. It catalyzes the removal of N-terminal methionine residues from nascent polypeptides, a process essential for protein maturation, stability, and functional regulation. By editing protein N-termini, METAP1 influences diverse cellular pathways, including angiogenesis, cell proliferation, and apoptosis. Dysregulation of METAP1 activity has been linked to pathological conditions such as cancer, cardiovascular diseases, and microbial infections, highlighting its potential as a therapeutic target.
Recombinant METAP1 protein is produced via genetic engineering, typically by expressing the METAP1 gene in bacterial (e.g., *E. coli*) or eukaryotic systems, followed by purification using affinity tags like His-tag. This engineered protein retains the enzymatic activity of native METAP1. enabling researchers to study its structural and functional properties in vitro. Its applications span drug discovery, biochemical assays, and structural studies, particularly in screening inhibitors that could modulate METAP1 activity for therapeutic purposes.
Studies using recombinant METAP1 have revealed its dual dependence on divalent metal ions (e.g., Co²⁺, Mn²⁺) for catalysis and provided insights into substrate specificity. Additionally, METAP1's role in regulating eukaryotic initiation factor 2α (eIF2α) phosphorylation underscores its broader impact on cellular stress responses. As research continues, METAP1 recombinant protein remains a vital tool for unraveling its biological significance and developing targeted therapies against METAP1-associated diseases.
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