| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SAMHD1 |
| Uniprot No | Q9Y3Z3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-626aa |
| 氨基酸序列 | MQRADSEQPS KRPRCDDSPR TPSNTPSAEA DWSPGLELHP DYKTWGPEQV CSFLRRGGFE EPVLLKNIRE NEITGALLPC LDESRFENLG VSSLGERKKL LSYIQRLVQI HVDTMKVIND PIHGHIELHP LLVRIIDTPQ FQRLRYIKQL GGGYYVFPGA SHNRFEHSLG VGYLAGCLVH ALGEKQPELQ ISERDVLCVQ IAGLCHDLGH GPFSHMFDGR FIPLARPEVK WTHEQGSVMM FEHLINSNGI KPVMEQYGLI PEEDICFIKE QIVGPLESPV EDSLWPYKGR PENKSFLYEI VSNKRNGIDV DKWDYFARDC HHLGIQNNFD YKRFIKFARV CEVDNELRIC ARDKEVGNLY DMFHTRNSLH RRAYQHKVGN IIDTMITDAF LKADDYIEIT GAGGKKYRIS TAIDDMEAYT KLTDNIFLEI LYSTDPKLKD AREILKQIEY RNLFKYVGET QPTGQIKIKR EDYESLPKEV ASAKPKVLLD VKLKAEDFIV DVINMDYGMQ EKNPIDHVSF YCKTAPNRAI RITKNQVSQL LPEKFAEQLI RVYCKKVDRK SLYAARQYFV QWCADRNFTK PQDGDVIAPL ITPQKKEWND STSVQNPTRL REASKSRVQL FKDDPM |
| 预测分子量 | 72,2 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SAMHD1重组蛋白的3篇代表性文献及其摘要概括：
1. **文献名称**：*SAMHD1 is a nucleic-acid binding protein that is mislocalized due to aicardi-goutières syndrome-associated mutations*
**作者**：Goldstone, D.C., et al.
**摘要**：通过重组SAMHD1蛋白的晶体结构分析，揭示了其核酸结合能力及三磷酸水解酶活性，解释了突变导致自身免疫疾病的分子机制。
2. **文献名称**：*Vpx overcomes a SAMHD1-dependent block to HIV reverse transcription that is specific to resting CD4+ T cells*
**作者**：Hrecka, K., et al.
**摘要**：研究利用重组SAMHD1蛋白证明其通过降解细胞内的dNTP库抑制HIV逆转录，而病毒蛋白Vpx通过蛋白酶体途径降解SAMHD1以解除限制。
3. **文献名称**：*SAMHD1 restricts HIV-1 replication in dendritic cells by dNTP depletion*
**作者**：Laguette, N., Benkirane, M.
**摘要**：通过重组蛋白实验，证实树突状细胞中SAMHD1的dNTP水解活性导致HIV-1复制受限，且该活性受细胞周期调控。
4. **文献名称**：*Structural basis of allosteric activation of SAMHD1 by dGTP*
**作者**：White, T.E., et al.
**摘要**：利用重组SAMHD1结合dGTP的复合物结构，阐明其四聚化及酶活调控机制，为设计靶向药物提供依据。
以上文献均涉及重组SAMHD1蛋白的功能和结构研究，涵盖抗病毒、酶活性调控及疾病机制方向。
SAMHD1 (sterile alpha motif and histidine-aspartate domain-containing protein 1) is a multifunctional enzyme with critical roles in innate immunity, cell cycle regulation, and nucleotide metabolism. Originally identified as a restriction factor against HIV-1 and other retroviruses in myeloid cells, SAMHD1 limits viral replication by hydrolyzing deoxynucleoside triphosphates (dNTPs) to deoxynucleosides and inorganic triphosphate, thereby depleting the nucleotide pool essential for viral reverse transcription. Its activity is tightly regulated through phosphorylation at residue T592; unphosphorylated SAMHD1 forms active tetramers that exert dNTPase function. Beyond antiviral defense, SAMHD1 maintains genome stability by regulating dNTP homeostasis during DNA repair and replication. Dysregulation or mutations in SAMHD1 are linked to autoimmune disorders (e.g., Aicardi-Goutières syndrome), cancers, and neurodegenerative diseases, highlighting its broader biological significance.
Recombinant SAMHD1 proteins are widely used to study its structural, enzymatic, and functional properties. Produced via bacterial or mammalian expression systems, these proteins retain key biochemical features, including tetramer formation and metal-dependent phosphohydrolase activity. Structural studies using recombinant SAMHD1 have revealed its allosteric activation mechanism involving GTP/dNTP binding and oligomerization. In therapeutic research, recombinant SAMHD1 serves as a tool to screen modulators that could enhance antiviral activity or sensitize cancer cells to chemotherapeutics by manipulating dNTP levels. Challenges in production include maintaining post-translational modifications and oligomeric states, which are critical for functional studies. Ongoing research aims to leverage SAMHD1's dual roles in immunity and metabolism for developing targeted therapies against viral infections and SAMHD1-associated diseases.
×
