Product Description
Size: 1Kit
UFL1 KO cell lysate available now. KO validated by. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 2 bp deletion in exon2 and 5 bp deletion in exon2 and 7 bp deletion in exon2.
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, 2 bp deletion in exon2 and 5 bp deletion in exon2 and 7 bp deletion in exon2.
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 and ERS Genomics Limited, and is developed with patented technology. For full details of the limited use licenses and relevant patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-UFL1, 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.
UFL1 also known as E3 ubiquitin-protein ligase UFL1 is a protein involved in the post-translational modification process called ufmylation. This protein has a molecular mass of approximately 34 kDa and facilitates the attachment of the ubiquitin-fold modifier 1 (UFM1) to target proteins. UFL1 is widely expressed in various tissues including the liver heart and kidney. It forms part of a complex that includes UFM1 UBA5 and UFC1 which are all essential for its function.
Biological function summary
UFL1 regulates proteins' stability and activity by ufmylation in the endoplasmic reticulum (ER) stress response. This protein modifies select substrates enhancing their role in maintaining cellular homeostasis under stress conditions. UFL1 works closely with UFM1 and is part of a complex that targets specific proteins indicating its role in maintaining proper cellular conditions during ER stress. This modification mechanism is important for cells to adapt to changing environments and sustain normal function.
Pathways
UFL1 plays a role in the ER stress response and protein folding pathways. It operates alongside other proteins including UFM1 which is critical in these processes. UFL1 modulates pathways linked with cellular responses to stress and survival. It interacts with proteins like CDK5 suggesting a role in cellular processes that require precise regulation during stress conditions. Such interactions further integrate UFL1 into overarching cellular survival strategies.
UFL1 has implications in cancer and neurodegenerative diseases. Dysregulation of ufmylation where UFL1 is an important player shows links to tumor progression and survival mechanisms in cancer. UFL1 is also connected to pathological protein aggregation relevant in neurodegenerative diseases. Its interaction with proteins involved in ER stress response suggests a relationship to these conditions. Understanding UFL1's function in these diseases is important for identifying therapeutic targets.
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Collaboration
Tony Tang
Email: Tony.Tang@iright.com
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