RNF34 Blocking Peptide | RNF34 (HGNC:17297) blocking peptide

RNF34 Antibody (C-term) Blocking Peptide

• Gene Names: RNF34; RFI; RIF; RIFF; hRFI; CARP1; CARP-1
• Synonyms: RNF34; RNF34 Antibody (C-term) Blocking Peptide; E3 ubiquitin-protein ligase RNF34; 632- ; Caspase regulator CARP1; Caspases-8 and -10-associated RING finger protein 1; CARP-1; FYVE-RING finger protein Momo; RNF34 (HGNC:17297) blocking peptide

• Form/Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
• Sequence Length: 372

• Cellular Location: Cell membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Nucleus. Nucleus speckle. Cytoplasm, cytosol
• Tissue Location: Ubiquitous. Detected in heart, brain, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, colon and leukocytes.
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for RNF34 (HGNC:17297) blocking peptide

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).

NCBI and Uniprot Product Information

• NCBI GI #: 74760679
• NCBI GeneID: 80196
• UniProt Accession #: Q969K3; Q8NG47; Q9H6W8; B7Z933
• Molecular Weight: 41,797 Da
• NCBI Official Full Name: E3 ubiquitin-protein ligase RNF34
• NCBI Official Synonym Full Names: ring finger protein 34
• NCBI Official Symbol: RNF34
• NCBI Official Synonym Symbols: RFI; RIF; RIFF; hRFI; CARP1; CARP-1
• NCBI Protein Information: E3 ubiquitin-protein ligase RNF34
• UniProt Protein Name: E3 ubiquitin-protein ligase RNF34
• UniProt Gene Name: RNF34
• UniProt Synonym Gene Names: hRFI
• UniProt Entry Name: RNF34_HUMAN

NCBI Description

The protein encoded by this gene contains a RINF finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein interacts with DNAJA3/hTid-1, which is a DnaJ protein reported to function as a modulator of apoptosis. Overexpression of this gene in Hela cells was shown to confer the resistance to TNF-alpha induced apoptosis, suggesting an anti-apoptotic function of this protein. This protein can be cleaved by caspase-3 during the induction of apoptosis. This protein also targets p53 and phospho-p53 for degradation. Alternatively splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Feb 2012]

Uniprot Description

RNF34: Has E3 ubiquitin-protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Protects cells against apoptosis induced by TNF. Binds phosphatidylinositol 5-phosphate and phosphatidylinositol 3- phosphate. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Ubiquitin conjugating system; Ligase; Ubiquitin ligase; EC 6.3.2.-

Chromosomal Location of Human Ortholog: 12q24.31

Cellular Component: cytoplasm; cytosol; nucleoplasm; nucleus; plasma membrane

Molecular Function: p53 binding; protein binding; ubiquitin protein ligase binding; ubiquitin-protein ligase activity

Biological Process: proteasomal ubiquitin-dependent protein catabolic process; protein polyubiquitination; protein ubiquitination; protein ubiquitination during ubiquitin-dependent protein catabolic process