Recombinant human Rffl protein (Active)
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Recombinant human Rffl protein (Active) is a Human Full Length protein, in the 1 to 363 aa range, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for SDS-PAGE, FuncS.
View Alternative Names
RNF189, RNF34L, RFFL, E3 ubiquitin-protein ligase rififylin, Caspase regulator CARP2, Caspases-8 and -10-associated RING finger protein 2, FYVE-RING finger protein Sakura, RING finger and FYVE-like domain-containing protein 1, RING finger protein 189, RING finger protein 34-like, RING-type E3 ubiquitin transferase rififylin, CARP-2, Fring
- FuncS
Supplier Data
Functional Studies - Recombinant human Rffl protein (Active) (AB268947)
The specific activity of ab268947 was 18 nmol/min/mg in a ubiquitinating assay using wild-type ubiquitin protein as substrate.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human Rffl protein (Active) (AB268947)
SDS-PAGE analysis of ab268947.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The Rffl protein participates in the regulation of innate immune responses. It facilitates the polyubiquitination of signaling molecules involved in antiviral pathways. Rffl is not part of a large complex itself but works closely with other proteins to enhance the activation of the immune system's antiviral responses. Its activity modulates the RIG-I-like receptor (RLR) signaling pathway important for the detection of viral RNA by interacting with essential signaling molecules like RIG-I and MAVS.
Pathways
Rffl acts within the signaling cascade related to the RLR pathway and the NF-kappaB pathway. These are essential in mounting an effective immune response against viral infections. Rffl influences the pathway by modulating the function of proteins like TRAF3 and TBK1. Through these interactions it affects the downstream production of type I interferons and other immune response mediators.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. Negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling.
Post-translational modifications
Autoubiquitinated.. Palmitoylated.. Undergoes caspase-mediated cleavage upon death-receptor activation, by TNFSF10 for instance. May be mediated by the caspases CASP8 and CASP10 in a negative feedback loop.
Subcellular localisation
Recycling endosome membrane
Product protocols
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Target data
Product promise
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