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BRAND / VENDOR: Abcam

Abcam, ab259227, Human UBE3B knockout HeLa cell lysate

CATALOG NUMBER: ab259227
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Product Description

Size: 1Kit
UBE3B KO cell lysate available now. KO validated by. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 4 bp deletion in exon3 and Insertion of the selection cassette in exon3.
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, 4 bp deletion in exon3 and Insertion of the selection cassette in exon3.,
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-UBE3B, 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.
UBE3B also known as ubiquitin-protein ligase E3B or hRPF1 is an enzyme that catalyzes the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate protein tagging it for degradation by the proteasome. It has a molecular weight of approximately 120 kDa. UBE3B is broadly expressed across various tissues including brain heart and muscles. The widespread expression pattern emphasizes its importance in protein homeostasis across different cell types.
Biological function summary
UBE3B functions as an important regulator in cellular processes by tagging damaged or unneeded proteins with ubiquitin directing them for degradation. This protein is not part of any known large macromolecular complex but works closely with other enzymes in the ubiquitination cascade especially E2 enzymes. Through this activity UBE3B helps control the quality of proteins within the cell aiding in the removal of proteins that could potentially be harmful.
Pathways
UBE3B plays a significant role in the ubiquitin-proteasome pathway which is pivotal for protein turnover and cellular regulation. Additionally UBE3B interacts with pathways involved in synaptic function highlighting its possible connection to neurological processes. It works alongside other ligases and deubiquitinating enzymes facilitating the maintenance of cellular protein levels and functions that are necessary for proper signaling and response in cells.
Mutations in UBE3B have been linked to neurological disorders including Kaufman oculocerebrofacial syndrome. This condition highlights the protein's involvement in brain development and function. UBE3B's ubiquitination activity connects it with proteins like SHANK3 which is also implicated in neurodevelopmental disorders. Therefore disturbances in UBE3B's function can have significant consequences for neural integrity and development.


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Collaboration

Tony Tang

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