Description
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, 1 bp insertion in exon15 and 2 bp deletion in exon15.,
Disease:Adenocarcinoma
Product details:
Knockout cell lysate achieved by CRISPR/Cas9.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Lysate preparation:
Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10).
This means that the protein of interest is denatured.
If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions:
Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-DNAJC13, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
RME-8 also known as DNAJC13 is a protein that functions as an ATPase assisting in the regulation of clathrin-mediated endocytosis. It possesses a mass of approximately 218 kDa and is mainly found in the central nervous system though it is also present in various other tissues. Mechanically RME-8 binds to clathrin-coated vesicles and plays a part in rearranging them during endocytosis. It interacts with multiple factors involved in membrane trafficking contributing to the modulation of vesicle fission and fusion events.
Biological function summary
The activity of RME-8 is essential for the maintenance of cellular homeostasis. It interacts with other proteins to form a complex that facilitates proper protein sorting within the endosomal network. RME-8's role in this intricate system ensures the appropriate recycling of receptors and disposal of damaged cellular components aiding in overall cell function. The protein regulates the spatial organization of endosomes an important process necessary for nutrient uptake and receptor recycling which impacts cell signaling and metabolism.
Pathways
RME-8 participates in endocytic pathways where it collaborates with proteins like Eps15 and Hsc70 to manage cargo trafficking. The endocytic pathway heavily relies on RME-8's functions for sustaining efficient internalization and routing of molecules such as receptors and ligands. Additionally the protein interacts with components of the retromer complex indicating a connection to the retromer-mediated transport pathway. This involvement may have effects on intracellular transport activities influencing the broader cellular communication network.
RME-8 has connections to neurodegenerative disorders such as Parkinson's disease. Mutations in the DNAJC13 gene which codes for RME-8 have been linked to familial parkinsonism. The dysfunction of RME-8 affects endosomal processes potentially contributing to the pathophysiology of Parkinson's by impacting dopamine neuron survival. It is also implicated in Alzheimer's disease with disruptions in its role possibly affecting amyloid-beta processing through its interactions with proteins like Sortilin-related receptor 1 (SORL1) which is known to influence amyloid precursor protein sorting and degradation.
