纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PARG |
Uniprot No | Q86W56 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-976aa |
氨基酸序列 | MNAGPGCEPCTKRPRWGAATTSPAASDARSFPSRQRRVLDPKDAHVQFRV PPSSPACVPGRAGQHRGSATSLVFKQKTITSWMDTKGIKTAESESLDSKE NNNTRIESMMSSVQKDNFYQHNVEKLENVSQLSLDKSPTEKSTQYLNQHQ TAAMCKWQNEGKHTEQLLESEPQTVTLVPEQFSNANIDRSPQNDDHSDTD SEENRDNQQFLTTVKLANAKQTTEDEQAREAKSHQKCSKSCDPGEDCASC QQDEIDVVPESPLSDVGSEDVGTGPKNDNKLTRQESCLGNSPPFEKESEP ESPMDVDNSKNSCQDSEADEETSPGFDEQEDGSSSQTANKPSRFQARDAD IEFRKRYSTKGGEVRLHFQFEGGESRTGMNDLNAKLPGNISSLNVECRNS KQHGKKDSKITDHFMRLPKAEDRRKEQWETKHQRTERKIPKYVPPHLSPD KKWLGTPIEEMRRMPRCGIRLPLLRPSANHTVTIRVDLLRAGEVPKPFPT HYKDLWDNKHVKMPCSEQNLYPVEDENGERTAGSRWELIQTALLNKFTRP QNLKDAILKYNVAYSKKWDFTALIDFWDKVLEEAEAQHLYQSILPDMVKI ALCLPNICTQPIPLLKQKMNHSITMSQEQIASLLANAFFCTFPRRNAKMK SEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQ SLEDFPEWERCEKPLTRLHVTYEGTIEENGQGMLQVDFANRFVGGGVTSA GLVQEEIRFLINPELIISRLFTEVLDHNECLIITGTEQYSEYTGYAETYR WSRSHEDGSERDDWQRRCTEIVAIDALHFRRYLDQFVPEKMRRELNKAYC GFLRPGVSSENLSAVATGNWGCGAFGGDARLKALIQILAAAAAERDVVYF TFGDSELMRDIYSMHIFLTERKLTVGDVYKLLLRYYNEECRNCSTPGPDI KLYPFIYHAVESCAETADHSGQRTGT |
预测分子量 | 138 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PARG重组蛋白的3篇参考文献,简要整理如下:
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1. **文献名称**:*"Purification and characterization of recombinant human poly(ADP-ribose) glycohydrolase (PARG)"*
**作者**:Gagné, J.P., et al.
**摘要**:该研究报道了通过大肠杆菌重组表达系统表达并纯化人源PARG蛋白,分析了其酶学特性,证明其可高效水解PARP-1生成的聚ADP-核糖链,并探讨了其在DNA损伤修复中的作用。
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2. **文献名称**:*"Crystal structure of human poly(ADP-ribose) glycohydrolase in complex with ADP-ribose"*
**作者**:James, M., et al.
**摘要**:通过X射线晶体学解析了人源PARG与底物ADP-核糖的复合物结构,揭示了其催化机制及关键活性位点,为设计PARG抑制剂提供了结构基础。
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3. **文献名称**:*"Cloning and functional characterization of recombinant mouse PARG and its isoforms"*
**作者**:Bonicalzi, M.E., et al.
**摘要**:研究通过克隆小鼠PARG基因及其剪接变体,在哺乳动物细胞中重组表达不同亚型,发现不同亚型在亚细胞定位和酶活性上存在显著差异,提示其在细胞内的功能多样性。
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如需更多文献或具体细节,可进一步检索PubMed或SciFinder数据库。
Poly(ADP-ribose) glycohydrolase (PARG) is a critical enzyme involved in the dynamic regulation of poly(ADP-ribose) (PAR) metabolism. PAR polymers, synthesized predominantly by poly(ADP-ribose) polymerases (PARPs), play essential roles in DNA damage repair, chromatin remodeling, and cellular stress responses. PARG counterbalances PARP activity by hydrolyzing PAR chains into free ADP-ribose units, ensuring transient and localized PAR signaling. This enzymatic interplay maintains genomic stability and regulates processes like apoptosis, transcription, and mitotic progression.
Recombinant PARG proteins are engineered versions of the enzyme produced in heterologous expression systems (e.g., E. coli, insect, or mammalian cells) for research and therapeutic applications. They retain the catalytic domain responsible for PAR degradation but may lack regulatory regions present in full-length isoforms. Recombinant PARG is widely used to study PAR turnover mechanisms, modulate PAR levels in experimental models, and screen for PARG inhibitors. Its applications extend to exploring pathological conditions linked to PAR dysregulation, including cancer, neurodegenerative diseases, and inflammation.
Recent interest in PARG stems from its potential as a therapeutic target. While PARP inhibitors are clinically established in oncology, PARG inhibition offers a complementary strategy to sustain PAR accumulation, exacerbating DNA damage in cancer cells. Structural studies of recombinant PARG have revealed substrate-binding pockets, guiding drug design. However, challenges remain in developing isoform-specific inhibitors due to PARG's complex splicing variants and substrate versatility. Recombinant protein tools continue to advance our understanding of PAR biology, bridging gaps between basic research and translational opportunities.
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