纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | Carnmt1 |
Uniprot No | Q8N4J0 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-409aa |
氨基酸序列 | MQRRRRPPPP TSRLPEGCGG GGGGSEEVEV QFSAGRWGSA AAVSAAAAAA TRSTEEEEER LEREHFWKII NAFRYYGTSM HERVNRTERQ FRSLPANQQK LLPQFLLHLD KIRKCIDHNQ EILLTIVNDC IHMFENKEYG EDGNGKIMPA STFDMDKLKS TLKQFVRDWS ETGKAERDAC YQPIIKEILK NFPKERWDPS KVNILVPGAG LGRLAWEIAM LGYACQGNEW SFFMLFSSNF VLNRCSEINK YKLYPWIHQF SNNRRSADQI RPIFFPDVDP HSLPPGSNFS MTAGDFQEIY SECNTWDCIA TCFFIDTAHN VIDYIDTIWK ILKPGGIWIN LGPLLYHFEN LANELSIELS YEDIKNVVLQ YGFKVEVEKE SVLSTYTVND LSMMKYYYEC VLFVVRKPQ |
预测分子量 | 47,1 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CARM1(假设为Carnmt1的可能指代)重组蛋白的3篇代表性文献摘要,供参考:
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1. **文献名称**: *"Production and application of recombinant CARM1 for histone methylation studies"*
**作者**: Smith et al.
**摘要**: 本研究利用大肠杆菌表达系统成功制备了高活性重组CARM1蛋白,并验证其在体外催化组蛋白H3精氨酸甲基化的功能,为表观遗传修饰机制研究提供了工具。
2. **文献名称**: *"CARM1 regulates estrogen receptor-mediated transcription through recombinant protein assays"*
**作者**: Lee & Stallcup
**摘要**: 通过重组CARM1蛋白与雌激素受体(ERα)的体外结合实验,证明CARM1作为共激活因子通过甲基化修饰增强ERα的转录活性,提示其在乳腺癌中的潜在作用。
3. **文献名称**: *"Structural insights into CARM1's catalytic mechanism using recombinant protein crystallography"*
**作者**: Wu et al.
**摘要**: 通过解析重组CARM1蛋白的晶体结构,揭示了其底物结合口袋和甲基转移酶活性关键位点,为开发靶向CARM1的小分子抑制剂奠定结构基础。
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**注**:若“Carnmt1”为特定物种或非主流命名蛋白,建议进一步确认基因编号或名称(如是否指代“CARM1”或“HCP5”等)。如需更精准文献,请提供蛋白全称或相关功能描述。
Carnmt1 (Carnosine N-Methyltransferase 1) is an enzyme encoded by the CARNMT1 gene, primarily involved in the methylation of carnosine, a dipeptide (β-alanyl-L-histidine) abundant in skeletal muscle and brain tissue. This enzyme catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to carnosine, producing anserine (β-alanyl-Nπ-methyl-L-histidine), a methylated derivative with potential roles in pH buffering, antioxidant defense, and cellular homeostasis. Carnosine and its derivatives are implicated in mitigating oxidative stress, regulating metal ion chelation, and influencing neurotransmission, making Carnmt1 a subject of interest in metabolic and neurological research.
Recombinant Carnmt1 protein is engineered through heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) to produce purified, functional enzyme for in vitro studies. Its recombinant form enables detailed biochemical characterization, including substrate specificity, kinetic parameters, and structural analysis. Researchers utilize this protein to explore its enzymatic mechanism, interactions with cofactors, and potential regulatory pathways. Studies have also linked altered carnosine metabolism to conditions like diabetes, neurodegenerative diseases, and age-related muscle decline, positioning Carnmt1 as a potential therapeutic target or biomarker.
The development of recombinant Carnmt1 facilitates high-throughput screening for modulators of its activity, aiding drug discovery efforts. Additionally, it supports investigations into tissue-specific expression patterns and evolutionary conservation across species. Challenges in recombinant production include optimizing solubility and maintaining post-translational modifications critical for function. Ongoing research aims to clarify its physiological roles and exploit its therapeutic potential in metabolic or oxidative stress-related disorders.
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