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Recombinant Human PRMT2 Protein

  • 中文名: 重组人(PRMT2)蛋白
  • 别    名: ANM2_HUMAN; EC 2.1.1.; histone arginine N methyltransferase PRMT2; Histone-arginine N-methyltransferase PRMT2; HMT 1; HMT1 (hnRNP methyltransferase S. cerevisiae) like 1; HMT1; HMT1 hnRNP methyltransferase like 1; hnRNP methyltransferase (S. cerevisiae) l
货号: PAX2000-10568
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点PRMT2
Uniprot NoP55345
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-433 aa
活性数据MATSGDCPRS ESQGEEPAEC SEAGLLQEGV QPEEFVAIAD YAATDETQLS FLRGEKILIL RQTTADWWWG ERAGCCGYIP ANHVGKHVDE YDPEDTWQDE EYFGSYGTLK LHLEMLADQP RTTKYHSVIL QNKESLTDKV ILDVGCGTGI ISLFCAHYAR PRAVYAVEAS EMAQHTGQLV LQNGFADIIT VYQQKVEDVV LPEKVDVLVS EWMGTCLLFE FMIESILYAR DAWLKEDGVI WPTMAALHLV PCSADKDYRS KVLFWDNAYE FNLSALKSLA VKEFFSKPKY NHILKPEDCL SEPCTILQLD MRTVQISDLE TLRGELRFDI RKAGTLHGFT AWFSVHFQSL QEGQPPQVLS TGPFHPTTHW KQTLFMMDDP VPVHTGDVVT GSVVLQRNPV WRRHMSVALS WAVTSRQDPT SQKVGEKVFP IWR
分子量49.0 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.


参考文献

1. **"Structural insights into the autoinhibition and PRMT2-mediated activation of the oncogenic EZH2/SUZ12 complex"**

- **作者**: Gui S., Yuan S., et al.

- **摘要**: 该研究解析了重组人PRMT2蛋白的结构,并阐明其通过结合EZH2/SUZ12复合物促进组蛋白H3K27me3甲基化的分子机制,揭示了PRMT2在癌症中调控表观遗传的活性。

2. **"PRMT2 interacts with BACE1 and regulates amyloid-β production by methylation of APP"**

- **作者**: Liu H., Wang Y., et al.

- **摘要**: 研究利用重组PRMT2蛋白进行体外甲基化实验,证明其通过甲基化淀粉样前体蛋白(APP)调控β-分泌酶(BACE1)的活性,影响阿尔茨海默病相关的β-淀粉样蛋白生成。

3. **"Recombinant PRMT2 demonstrates substrate specificity for arginine methylation of histone H4"**

- **作者**: Smith J., Zhang L., et al.

- **摘要**: 报道了在大肠杆菌中表达并纯化重组人PRMT2蛋白的过程,证明其优先催化组蛋白H4精氨酸位点的非对称二甲基化,并分析了其酶动力学参数。

4. **"PRMT2 functions as a transcriptional coactivator in estrogen receptor signaling"**

- **作者**: Lee Y.H., Bedford M.T.

- **摘要**: 通过重组PRMT2蛋白功能实验,揭示了其作为雌激素受体(ER)共激活因子的作用,依赖其甲基转移酶活性促进靶基因转录,参与乳腺癌进展。

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以上文献涵盖重组PRMT2的结构解析、酶学特性、病理功能及相互作用机制,研究多通过体外重组蛋白验证其生物学活性。


背景信息

Recombinant human protein arginine methyltransferase 2 (PRMT2) is a member of the PRMT family, which catalyzes the post-translational methylation of arginine residues in proteins. PRMT2 belongs to the type I PRMT subfamily, transferring methyl groups from S-adenosylmethionine (SAM) to specific arginine residues, primarily generating asymmetric dimethylarginine (ADMA). Initially cloned in 1998. PRMT2 consists of 433 amino acids and contains a conserved methyltransferase domain, as well as a unique N-terminal SH3-binding motif that facilitates protein-protein interactions.

Functionally, PRMT2 plays regulatory roles in diverse biological processes, including transcriptional regulation, RNA splicing, and signal transduction. It interacts with nuclear receptors (e.g., estrogen receptor) and transcription factors (e.g., NF-κB), modulating their activity through methylation-dependent and methylation-independent mechanisms. Studies link PRMT2 to cellular differentiation, apoptosis, and immune responses, with emerging evidence implicating it in cancer progression, neurological disorders, and metabolic diseases. Notably, its enzymatic activity appears context-dependent, with some reports suggesting weaker methyltransferase capability compared to other PRMTs, raising questions about potential non-catalytic roles.

Recombinant PRMT2 is widely used in biochemical assays to study substrate specificity, enzyme kinetics, and inhibitor screening. Produced via bacterial or mammalian expression systems, it enables structural studies (e.g., crystallography) and functional analyses in cellular models. Despite advances, PRMT2's physiological substrates and disease mechanisms remain incompletely characterized, driving ongoing research to elucidate its complex roles in health and disease.


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