纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | PADI4 |
Uniprot No | Q9UM07 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-663aa |
氨基酸序列 | MAQGTLIRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVV DIAHGPPAKK KSTGSSTWPLDPGVEVTLTMKVASGSTGDQKVQISYYG PKTPPVKALLYLTGVEISLCAD ITRTGKVKPTRAVKDQRTWTWGPCGQ GAILLVNCDRDNLESSAMDCEDDEVLDSEDLQDM SLMTLSTKTPKDFF TNHTLVLHVARSEMDKVRVFQATRGKLSSKCSVVLGPKWPSHYLMV PG GKHNMDFYVEALAFPDTDFPGLITLTISLLDTSNLELPEAVVFQDSVVFR VAPWIMTP NTQPPQEVYACSIFENEDFLKSVTTLAMKAKCKLTICPEE ENMDDQWMQDEMEIGYIQAP HKTLPVVFDSPRNRGLKEFPIKRVMGPD FGYVTRGPQTGGISGLDSFGNLEVSPPVTVRG KEYPLGRILFGDSCYP SNDSRQMHQALQDFLSAQQVQAPVKLYSDWLSVGHVDEFLSFVP APDR KGFRLLLASPRSCYKLFQEQQNEGHGEALLFEGIKKKKQQKIKNILSNKT LREHNS FVERCIDWNRELLKRELGLAESDIIDIPQLFKLKEFSKAEAF FPNMVNMLVLGKHLGIPK PFGPVINGRCCLEEKVCSLLEPLGLQCTFI NDFFTYHIRHGEVHCGTNVRRKPFSFKWWN MVP |
预测分子量 | 75 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PADI4重组蛋白的3篇参考文献示例(注:文献信息为模拟概括,仅供参考):
1. **文献名称**: *"Recombinant human PADI4: Expression, purification, and enzymatic characterization"*
**作者**: Wang Y, et al.
**摘要**: 研究报道了人源PADI4重组蛋白在大肠杆菌中的高效表达与纯化方法,分析了其体外催化组蛋白H3精氨酸残基脱亚胺的酶活性和最适反应条件,为后续功能研究提供基础工具。
2. **文献名称**: *"PADI4-mediated citrullination promotes tumor progression in breast cancer models"*
**作者**: Chang X, et al.
**摘要**: 通过重组PADI4蛋白处理细胞,发现其诱导的蛋白质瓜氨酸化修饰通过激活NF-κB通路促进乳腺癌细胞侵袭和转移,提示PADI4可能成为癌症治疗靶点。
3. **文献名称**: *"Structural basis of histone H3 citrullination by PADI4"*
**作者**: Slade DJ, et al.
**摘要**: 利用重组PADI4蛋白进行X射线晶体学研究,揭示了PADI4与组蛋白H3结合的分子机制,阐明了其底物识别及催化精氨酸转化为瓜氨酸的结构基础。
(注:以上文献为示例性概括,实际文献需通过学术数据库查询确认。)
**Background of PADI4 Recombinant Protein**
Peptidylarginine deiminase 4 (PADI4) is a calcium-dependent enzyme belonging to the PADI family, which catalyzes the post-translational conversion of arginine residues to citrulline in proteins—a process termed citrullination. This modification alters protein structure and function, influencing diverse biological processes, including gene regulation, immune response, and epigenetic modulation. PADI4 is notably expressed in immune cells (e.g., neutrophils, macrophages) and certain cancer cells, where it plays roles in inflammation, autoimmunity, and tumorigenesis.
The recombinant PADI4 protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable in vitro studies. It retains enzymatic activity, allowing researchers to investigate citrullination mechanisms, substrate specificity, and interactions with inhibitors. Structurally, PADI4 contains an N-terminal regulatory domain, a central catalytic domain with conserved residues (Cys645. His471. Asp463) critical for catalysis, and a C-terminal domain involved in calcium binding and structural stability.
Research on recombinant PADI4 is pivotal in autoimmune diseases, particularly rheumatoid arthritis (RA), where aberrant citrullination of proteins triggers autoantibody production (e.g., anti-citrullinated protein antibodies, ACPAs). It also links to cancer progression by modulating histone citrullination, thereby affecting chromatin structure and gene __expression (e.g., suppressing tumor suppressor genes). Additionally, PADI4 is implicated in neutrophil extracellular trap (NET) formation, a defense mechanism that may exacerbate inflammation.
Pharmaceutically, recombinant PADI4 serves as a tool for drug screening, aiming to develop inhibitors targeting its catalytic activity. Such inhibitors hold therapeutic potential for RA, cancer, and other citrullination-driven pathologies. Understanding PADI4's molecular mechanisms through recombinant protein studies continues to advance insights into disease pathways and therapeutic interventions.
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