Recombinant Human RNF34 protein (His tag N-Terminus)
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Recombinant Human RNF34 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 373 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
E3 ubiquitin-protein ligase RNF34, Caspase regulator CARP1, Caspases-8 and -10-associated RING finger protein 1, FYVE-RING finger protein Momo, Human RING finger homologous to inhibitor of apoptosis protein, RING finger protein 34, RING finger protein RIFF, RING-type E3 ubiquitin transferase RNF34, CARP-1, hRFI, RNF34
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human RNF34 protein (His tag N-Terminus) (AB176063)
15% SDS-PAGE analysis of ab176063 (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
General info
Function
E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. 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 (PubMed : 15069192). May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation (PubMed : 17121812). Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN (PubMed : 18382127). Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells (PubMed : 22064484). Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation (PubMed : 25012219).
Post-translational modifications
Autoubiquitinated (in vitro).. Proteolytically cleaved by caspases upon induction of apoptosis by TNF.
Subcellular localisation
Nucleus
Target data
Product promise
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