Rabbit polyclonal primary
ITCH Rabbit Polyclonal Antibody (ER1901-94)
Recombinant protein within human itch aa 300-500.
Siha cell lysates, Mouse pancreatic tissue lysates, Hela, LOVO, Siha, Human liver cancer tissue, rat brain tissue, mouse pancreas tissue.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
Predicted band size 102/98/86 kDa.
ADMFD antibody; AIF4 antibody; AIP4 antibody; Atrophin 1 interacting protein 4 antibody; Atrophin-1-interacting protein 4 antibody; dJ468O1.1 antibody; dJ468O1.1 (atrophin 1 interacting protein 4 (AIP4)) antibody; dJ468O1.1 atrophin 1 interacting protein 4 AIP4 antibody; E3 ubiquitin protein ligase Itchy homolog antibody; E3 ubiquitin-protein ligase Itchy homolog antibody; EC 6.3.2 antibody; Itch antibody; ITCH_HUMAN antibody; Itchy E3 ubiquitin protein ligase antibody; Itchy E3 ubiquitin protein ligase homolog antibody; Itchy E3 ubiquitin protein ligase homolog mouse antibody; Itchy E3 ubiquitin protein ligase, mouse, homolog of antibody; Itchy homolog E3 ubiquitin protein ligase antibody; Itchy mouse homolog E3 ubiquitin protein ligase antibody; NAPP1 antibody; NFE2 associated polypeptide 1 antibody; NFE2-associated polypeptide 1 antibody; Ubiquitin protein ligase ITCH antibody
On T-cell activation, phosphorylation by the JNK cascade on serine and threonine residues surrounding the PRR domain accelerates the ubiquitination and degradation of JUN and JUNB. The increased ITCH catalytic activity due to phosphorylation by JNK1 may occur due to a conformational change disrupting the interaction between the PRR/WW motifs domain and the HECT domain and, thus exposing the HECT domain (By similarity). Phosphorylation by FYN reduces interaction with JUNB and negatively controls JUN ubiquitination and degradation.; Monoubiquitinated. Autopolyubiquitinated with 'Lys-63' linkages which does not lead to protein degradation.
Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus.
Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . Involved in the control of inflammatory signaling pathways . Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways . Promotes the association of the complex after TNF stimulation . Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains . This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response . Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages .