|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. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. It is involved in the control of inflammatory signaling pathways. Is an 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. Critical regulator of T-helper (TH2) cytokine development through its ability to induce JUNB ubiquitination and degradation (By similarity). Ubiquitinates SNX9. Ubiquitinates CXCR4 and HGS/HRS and regulates sorting of CXCR4 to the degradative pathway. It is involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination.|
|Cellular Location||Cell membrane. Cytoplasm. Nucleus. Note=Associates with endocytic vesicles. May be recruited to exosomes by NDFIP1|
|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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