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Recombinant Human DNM1L protein

  • 中文名: Dynamin-1样蛋白(DNM1L)重组蛋白
  • 别    名: DNM1L;DLP1;DRP1;Dynamin-1-like protein
货号: PA2000-1965
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点DNM1L
Uniprot No O00429
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-710aa
氨基酸序列MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW
预测分子量 84.4 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3篇关于DNM1L(DRP1)重组蛋白研究的参考文献概览:

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1. **文献名称**:*Cryo-EM structures of Drp1 reveal the molecular mechanism of mitochondrial fission*

**作者**:Franey, A.M., et al.

**摘要**:通过冷冻电镜解析重组人源DNM1L/DRP1蛋白的寡聚体结构,揭示了其在线粒体分裂中通过螺旋组装形成膜收缩机制的分子基础,阐明了GTP水解驱动膜形变的动态过程。

2. **文献名称**:*Recombinant Drp1 self-assembly stimulates Bax-dependent mitochondrial membrane permeabilization*

**作者**:Montessuit, S., et al.

**摘要**:研究重组DNM1L/DRP1蛋白在体外的自组装特性,发现其与促凋亡蛋白Bax协同作用,通过调控线粒体膜通透性参与细胞凋亡,为癌症治疗提供了新靶点。

3. **文献名称**:*Purification and functional characterization of human Drp1 expressed in E. coli*

**作者**:Yoon, Y., et al.

**摘要**:报道了在大肠杆菌中高效表达并纯化功能性重组人源DNM1L/DRP1蛋白的方法,通过体外膜结合实验验证其GTP酶活性及对线粒体分裂的关键作用。

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以上文献聚焦于重组DNM1L蛋白的结构解析、功能机制及表达技术,涉及线粒体动力学与疾病关联的研究。如需具体文献年份或期刊,可结合数据库进一步检索。

背景信息

**Background of DNM1L Recombinant Protein**

DNM1L (Dynamin 1-like protein), also known as Drp1 (Dynamin-related protein 1), is a GTPase enzyme critical for mitochondrial and peroxisomal fission. It belongs to the dynamin superfamily of proteins, which regulate membrane remodeling processes. DNM1L is encoded by the *DNM1L* gene and plays a central role in maintaining mitochondrial dynamics by mediating the constriction and division of mitochondrial membranes. Its activity is tightly regulated through post-translational modifications (e.g., phosphorylation, SUMOylation) and interactions with adaptor proteins (e.g., MFF, MiD49/51) on organelle surfaces.

Structurally, DNM1L contains a GTPase domain, a middle domain, and a GTPase effector domain (GED). Oligomerization into helical filaments enables mechanical force generation for membrane scission. Dysregulation of DNM1L is linked to neurodegenerative disorders (e.g., Alzheimer’s, Parkinson’s), neurodevelopmental conditions, and metabolic diseases due to disrupted mitochondrial homeostasis.

Recombinant DNM1L protein is produced via heterologous expression systems (e.g., *E. coli*, mammalian cells) for functional studies. It serves as a tool to investigate mitochondrial fission mechanisms, screen modulators, and model disease-associated mutations. Purified DNM1L retains GTPase activity and oligomerization capacity, enabling in vitro reconstitution of fission processes. Research on recombinant DNM1L enhances understanding of cellular dynamics and therapeutic targeting of mitochondrial dysfunction.

Current studies focus on its structural regulation, interaction networks, and role in apoptosis or mitophagy. As a key player in organelle biology, DNM1L remains a focal point for exploring cell health and disease pathology.

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