| 纯度 | >80%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SIRT6 |
| Uniprot No | Q8N6T7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | Met1~Ser355 |
| 氨基酸序列 | MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSSSWVFHTGAGISTASGIPDFR GPHGVWTMEERGL APKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHVRSGFPRD KL AELHGNMFVEECAKCKTQYVRDTVVGTMGL KATGRLCTVAKARGLRACRGEL RDTILDWE DSLPDRDL ALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRHADLRI HGYVDEVMTRLMKHLGLEIPAWDGPRVLERALPPLPRPPTPKLEPKEESPTRINGSIPAGPKQEP CAQHNGSEPASPKRERPTSPAPHRPPKRVKAKAVPS |
| 预测分子量 | 42.8kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% Sarcosyl, 5% Trehalose |
| 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. |
1. **"SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine"**
*作者：Jiang, H., et al. (2013).*
摘要：该研究揭示了SIRT6通过去脂肪酰化修饰调控TNF-α分泌的分子机制，利用重组SIRT6蛋白证明其具有水解长链脂肪酰基赖氨酸的酶活性，并参与炎症反应调控。
2. **"Crystal structure of the SIRT6 deacetylase reveals a novel regulatory mechanism"**
*作者：Pan, P.W., et al. (2011).*
摘要：通过解析SIRT6重组蛋白的晶体结构，发现其独特的锌指结构域和底物结合口袋特征，揭示了SIRT6依赖NAD+的去乙酰化酶活性及在染色质沉默中的作用机制。
3. **"SIRT6 promotes DNA repair under stress by activating PARP1"**
*作者：Mao, Z., et al. (2011).*
摘要：研究发现重组SIRT6蛋白通过单ADP-核糖基化修饰激活PARP1.增强DNA损伤修复能力，并证明其在氧化应激下维持基因组稳定的关键功能。
4. **"The sirtuin SIRT6 regulates lifespan in male mice"**
*作者：Kanfi, Y., et al. (2012).*
摘要：利用过表达SIRT6重组蛋白的转基因小鼠模型，证明SIRT6通过调控代谢通路和应激响应延长雄性小鼠寿命，为衰老干预提供新靶点。
SIRT6. a member of the sirtuin family of NAD⁺-dependent deacetylases and ADP-ribosyltransferases, is a conserved enzyme implicated in critical biological processes, including genome stability, DNA repair, metabolic regulation, and aging. Initially identified for its role in chromatin modification, SIRT6 specifically targets histone H3 lysine 9 (H3K9) and lysine 56 (H3K56), influencing transcriptional silencing and DNA damage response. Beyond epigenetic regulation, SIRT6 modulates glucose and lipid metabolism by interacting with key transcription factors like HIF-1α and NF-κB, thereby linking cellular energy status to stress resistance and longevity.
Recombinant SIRT6 protein, produced via bacterial (e.g., *E. coli*) or mammalian expression systems, is a vital tool for studying its enzymatic activities and molecular mechanisms. Purification typically involves affinity chromatography (e.g., His-tag or GST-tag systems) followed by functional validation through deacetylation or ADP-ribosylation assays. Its recombinant form enables high-throughput screening for activators or inhibitors, which hold therapeutic potential for age-related diseases, cancer, and metabolic disorders.
Research highlights SIRT6's dual role in cancer: it suppresses tumorigenesis by stabilizing genomes and repressing oncogenic pathways but may promote cancer cell survival under stress. In aging models, SIRT6 overexpression extends lifespan and mitigates degenerative phenotypes, partly by enhancing DNA repair and reducing inflammation. Recent studies also explore its involvement in neurodegeneration, cardiovascular diseases, and immune regulation. Despite progress, challenges remain in understanding tissue-specific functions, post-translational modifications, and optimal delivery strategies for therapeutic applications. Recombinant SIRT6 continues to bridge gaps between biochemical insights and translational opportunities in precision medicine.
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