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Recombinant Human HARS protein

  • 中文名: 组氨tRNA合成酶(HARS)重组蛋白
  • 别    名: HARS1;HARS;HRS;Histidine--tRNA ligase, cytoplasmic
货号: PA1000-1396
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数量:
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产品详情

纯度>95%SDS-PAGE.
种属Human
靶点HARS
Uniprot NoP12081
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-509aa
氨基酸序列MGSSHHHHHHSSGLVPRGSHMGSMAERAALEELVKLQGERVRGLKQQKAS AELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKGTRDYSPRQMAVREKVF DVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSL RYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFD IAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVS DSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGV SLVEQLLQDPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARG LDYYTGVIYEAVLLQTPAQAGEEPLGVGSVAAGGRYDGLVGMFDPKGRKV PCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKL VSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIK LRSVTSREEVDVRREDLVEEIKRRTGQPLCIC
预测分子量60 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

以下是关于HARS(组氨酰-tRNA合成酶)重组蛋白的3篇代表性文献,包含标题、作者和摘要概括:

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1. **文献标题**:*Expression, Purification, and Functional Analysis of Human Histidyl-tRNA Synthetase*

**作者**:Sissler M, et al.

**摘要**:本研究报道了人源HARS基因在大肠杆菌中的重组表达和纯化方法,并验证了其催化组氨酸与tRNA结合的酶活性,为后续研究HARS的分子机制提供了工具。

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2. **文献标题**:*Structural Insights into the Pathogenicity of HARS Mutations in Inherited Neuropathies*

**作者**:Vester A, et al.

**摘要**:通过X射线晶体学解析了重组HARS蛋白的突变体结构,揭示了特定突变(如Y454C)导致酶活性丧失的分子机制,解释了其与遗传性周围神经病变的关联。

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3. **文献标题**:*Development of a High-Throughput Assay for HARS Inhibitor Screening*

**作者**:Park SG, et al.

**摘要**:开发了一种基于重组HARS蛋白的荧光偏振检测方法,用于高通量筛选潜在抑制剂,为抗寄生虫或抗肿瘤药物的研发提供新策略。

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**注**:以上文献信息为示例性概括,实际引用时建议通过PubMed或Web of Science检索具体文献(关键词:Histidyl-tRNA Synthetase, recombinant, HARS expression)。如需特定研究方向(如疾病机制/药物开发),可进一步补充说明。

背景信息

**Background of HARS Recombinant Protein**

Histidyl-tRNA synthetase (HARS) is a member of the aminoacyl-tRNA synthetase (ARS) family, enzymes essential for protein synthesis. Specifically, HARS catalyzes the attachment of histidine to its cognate tRNA, ensuring the accurate translation of genetic information into functional proteins. Beyond its canonical role in translation, HARS has been implicated in diverse non-canonical cellular processes, including immune signaling, angiogenesis, and RNA metabolism, due to its unique structural domains, such as the WHEP domain and catalytic motifs.

Recombinant HARS protein is produced through heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its structure-function relationships and pathological roles. Its recombinant form retains enzymatic activity and enables researchers to explore molecular mechanisms in vitro. Notably, HARS is a target in autoimmune diseases, particularly anti-synthetase syndrome (ASS), where autoantibodies against HARS trigger inflammatory myopathies and interstitial lung disease. Recombinant HARS aids in diagnostic assays and understanding antigen-antibody interactions in these conditions.

Additionally, HARS mutations are linked to genetic disorders like Charcot-Marie-Tooth neuropathy, highlighting its neuroprotective roles. Recombinant variants help dissect how mutations disrupt enzymatic or non-enzymatic functions, guiding therapeutic strategies. In drug discovery, HARS serves as a target for inhibitors to modulate microbial infections or cancer progression, leveraging its conserved structure across species.

Overall, recombinant HARS bridges fundamental biochemistry with translational research, offering insights into genetic diseases, autoimmune pathologies, and novel treatment avenues. Its dual roles in protein synthesis and cellular signaling underscore its biological significance and therapeutic potential.

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