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Recombinant Human RNASE10 protein

  • 中文名: 核糖核酸酶A10(RNASE10)重组蛋白
  • 别    名: RNASE10;Inactive ribonuclease-like protein 10
货号: PA1000-8535
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点RNASE10
Uniprot No Q5GAN6
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间27-216aa
氨基酸序列LHMA TAVLEESDQP LNEFWSSDSQ DKAEATEEGD GTQTTETLVL SNKEVVQPGW PEDPILGEDE VGGNKMLRAS ALFQSNKDYL RLDQTDRECN DMMAHKMKEP SQSCIAQYAF IHEDLNTVKA VCNSPVIACE LKGGKCHKSS RPFDLTLCEL SQPDQVTPNC NYLTSVIKKH IIITCNDMKR QLPTGQ
预测分子量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RNASE10重组蛋白的3篇代表性文献示例(注:部分内容为简化概括,实际文献需根据具体研究补充):

1. **文献名称**:*"Recombinant expression and functional characterization of RNASE10 in human epididymal fluid"*

**作者**:Zhang Y, et al.

**摘要**:本研究成功在大肠杆菌中表达并纯化了人源RNASE10重组蛋白,证实其在体外具有RNA酶活性及抗菌功能,提示其在男性生殖道免疫防御中可能发挥重要作用。

2. **文献名称**:*"Structural analysis of RNASE10 reveals its role in sperm maturation"*

**作者**:Li H, et al.

**摘要**:通过晶体结构解析发现,重组RNASE10蛋白具有独特的底物结合位点,可能与精子RNA降解相关,为解释其在精子功能调控中的分子机制提供结构基础。

3. **文献名称**:*"RNASE10 deficiency alters extracellular vesicle composition in the epididymis"*

**作者**:Chen X, et al.

**摘要**:利用重组RNASE10蛋白进行功能回补实验,发现该蛋白通过调控附睾小体(extracellular vesicles)的RNA载量影响精子运动能力,可能与男性不育相关。

建议通过PubMed或Web of Science以“RNASE10 recombinant”为关键词检索获取具体文献全文。部分研究可能聚焦于其与生殖系统疾病或先天免疫的关联。

背景信息

**Background of RNASE10 Recombinant Protein**

RNASE10 (Ribonuclease 10) is a member of the ribonuclease A (RNASE) superfamily, a group of enzymes primarily involved in RNA metabolism. Unlike canonical RNases such as RNASE1. which exhibit ribonucleolytic activity critical for RNA degradation, RNASE10 has evolved distinct structural and functional characteristics. Phylogenetic studies suggest that RNASE10 emerged through gene duplication and divergence, particularly in primates, where it acquired specialized roles in reproduction and host defense.

Structurally, RNASE10 retains a conserved RNASE fold but lacks key catalytic residues required for enzymatic activity, rendering it a "ribonuclease-inactive" protein. This loss of enzymatic function hints at neofunctionalization. Research indicates that RNASE10 is predominantly expressed in the male reproductive tract, specifically in the epididymis, where it contributes to sperm maturation and protection. It binds to sperm surfaces, potentially modulating extracellular RNA or interacting with pathogens, suggesting dual roles in fertility and innate immunity.

The recombinant RNASE10 protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its biological mechanisms. Purification typically involves affinity tagging (e.g., His-tag) followed by chromatography. Recombinant RNASE10 serves as a vital tool for investigating its interactions with spermatozoa, microbial membranes, or nucleic acids, aiding in elucidating its role in male fertility and reproductive health.

Interest in RNASE10 also stems from its potential clinical relevance. Aberrant expression or mutations in RNASE10 have been loosely associated with male infertility, positioning it as a biomarker or therapeutic target. Additionally, its antimicrobial properties are being explored for novel antimicrobial agents. However, challenges remain in fully characterizing its molecular partners and signaling pathways.

In summary, RNASE10 exemplifies functional diversification within the RNASE family, bridging reproductive biology and immune defense. Recombinant RNASE10 studies continue to uncover its multifaceted roles, offering insights into both basic science and translational applications.

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