|Application ||WB, E|
|Other Accession||NP_001244066, 380420335|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||Predicted: 99 kDa |
Observed: 99 kDa
|Application Notes||ITCH antibody can be used for detection of ITCH by Western blot at 1 - 2 µg/ml.|
|Target/Specificity||ITCH; ITCH antibody is human, mouse and rat reactive. At least three isoforms of ITCH are known to exist; this antibody only recognizes the two longest isoforms. This antibody is predicted to not cross-react with other members of the Nedd4 protein family.|
|Reconstitution & Storage||ITCH antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.|
|Precautions||ITCH Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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 (PubMed:14602072, PubMed:17028573, PubMed:16387660, PubMed:18718448, PubMed:18718449, PubMed:11046148, PubMed:19592251, PubMed:19116316, PubMed:19881509, PubMed:20491914, PubMed:20392206, PubMed:20068034, PubMed:23146885, PubMed:24790097, PubMed:25631046). Catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation (PubMed:17028573, PubMed:18718448, PubMed:19131965, PubMed:19881509). Involved in the control of inflammatory signaling pathways (PubMed:19131965). Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways (PubMed:19131965). Promotes the association of the complex after TNF stimulation (PubMed:19131965). Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains (PubMed:19131965). This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1 (PubMed:19131965). Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways (PubMed:19592251). Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response (PubMed:18718448, PubMed:20491914). Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages (PubMed:18718448). Mediates JUN ubiquitination and degradation (By similarity). Mediates JUNB ubiquitination and degradation (PubMed:16387660). Critical regulator of type 2 helper T (Th2) cell cytokine production by inducing JUNB ubiquitination and degradation (By similarity). Involved in the negative regulation of MAVS-dependent cellular antiviral responses (PubMed:19881509). Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation (PubMed:19881509). Following ligand stimulation, regulates sorting of Wnt receptor FZD4 to the degradative endocytic pathway probably by modulating PI42KA activity (PubMed:23146885). Ubiquitinates PI4K2A and negatively regulates its catalytic activity (PubMed:23146885). Ubiquitinates chemokine receptor CXCR4 and regulates sorting of CXCR4 to the degradative endocytic pathway following ligand stimulation by ubiquitinating endosomal sorting complex required for transport ESCRT-0 components HGS and STAM (PubMed:14602072, PubMed:23146885). Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination (PubMed:17028573, PubMed:18628966, PubMed:23886940). Ubiquitinates SNX9 (PubMed:20491914). Ubiquitinates MAP3K7 through 'Lys-48'- linked conjugation (By similarity). Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP (PubMed:20068034). Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID (PubMed:20392206). Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046).|
|Cellular Location||Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Nucleus. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Note=May be recruited to exosomes by NDFIP1 (PubMed:18819914). Localizes to plasma membrane upon CXCL12 stimulation where it co-localizes with CXCL4 (PubMed:14602072). Localization to early endosomes is increased upon CXCL12 stimulation where it co-localizes with DTX3L and CXCL4 (PubMed:24790097).|
|Tissue Location||Widely expressed.|
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Provided below are standard protocols that you may find useful for product applications.
The Itchy E3 ubiquitin protein ligase (ITCH) is a member of the Nedd4 family of HECT domain E3 ubiquitin ligases (1). HECT domain E3 ubiquitin ligases transfer ubiquitin from E2 ubiquitin-conjugating enzymes to protein substrates, thus targeting specific proteins for lysosomal degradation. ITCH plays a role in multiple cellular processes including erythroid and lymphoid cell differentiation and the regulation of immune responses (2). In B cells, ITCH is thought to associate with latent membrane protein 2A (LMP2A) of Epstein-Barr virus, specifically down-regulating its activity in B cell signaling (3). Mutations in this gene are a cause of syndromic multisystem autoimmune disease (4).
Perry WL, Hustad CM, Swing DA, et al. The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice. Nat. Genet. 1998; 18:143-6.
Melino G, Gallagher E, Aqeilan RI, et al. Itch: a HECT-type E3 ligase regulating immunity, skin and cancer. Cell Death Differ. 2008; 15:1103-12.
Ikeda A, Caldwell RG, Longnecker R, et al. Itchy, a Nedd4 ubiquitin ligase, downregulates latent membrane protein 2A activity in B-cell signaling. J. Virol. 2003; 77:5529-34.
Matesic LE, Copeland NG, and Jenkins NA. Itchy mice: the identification of a new pathway for the development of autoimmunity. Curr. Top. Microbiol. Immunol. 2008; 321:185-200.
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