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BRAND / VENDOR: Abcam

Abcam, ab259207, Human TRIM38 knockout A549 cell lysate

CATALOG NUMBER: ab259207
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Product Description

Size: 1Kit
TRIM38 KO cell lysate available now. KO validated by. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 1 bp insertion in exon5.
Key facts
Cell type:A549,
Species or organism:Human,
Tissue:Lung,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, 1 bp insertion in exon5.,
Disease:Carcinoma

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-TRIM38, 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.
TRIM38 also known as RNF15 is a member of the tripartite motif family characterized by its RING B-box and coiled-coil domains. It has a molecular mass of approximately 58 kDa. The structure of these domains suggests it functions in protein ubiquitination. TRIM38 is expressed in various tissues with notable expression in the immune system and skeletal tissues. Through these domains TRIM38 can mediate protein-protein interactions and potentially influence protein stability.
Biological function summary
The TRIM38 protein modulates immune responses. It does not form part of a complex but can act independently to regulate inflammatory signals. By targeting signaling proteins for ubiquitination TRIM38 plays a role in innate immunity influencing the production of inflammatory cytokines. This function is essential for keeping the immune response balanced and preventing excessive inflammation that can lead to tissue damage.
Pathways
TRIM38 influences the NF-kB and type I interferon pathways. These pathways are important in immune response modulation. In the NF-kB pathway TRIM38 controls the degradation of particular inhibitor proteins allowing the activation of this transcription factor which regulates genes involved in immune and inflammatory responses. TRIM38 also shares pathway interactions with proteins like TRAF6 and NEMO which contribute to its role in controlling the magnitude of these signaling cascades.
TRIM38 has associations with autoimmune diseases and inflammatory conditions. Abnormal regulation of its ubiquitination function can contribute to the pathogenesis of conditions like rheumatoid arthritis and systemic lupus erythematosus. In these diseases TRIM38's interaction with proteins like TRAF6 and interferon regulatory factors becomes imbalanced potentially leading to chronic inflammation and autoimmunity. Understanding TRIM38's role could provide insights for therapeutic interventions in related disorders.


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Collaboration

Tony Tang

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