|Application ||WB, E|
|Other Accession||NP_113671, 83737, 16396 (mouse), 311567 (rat)|
|Predicted||Mouse, Rat, Dog|
|Calculated MW||102803 Da|
|Other Names||E3 ubiquitin-protein ligase Itchy homolog, Itch, 6.3.2.-, Atrophin-1-interacting protein 4, AIP4, NFE2-associated polypeptide 1, NAPP1, ITCH|
|Format||0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Goat Anti-ITCH / AIF4 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. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046).|
|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.
Atrophin-1 contains a polyglutamine repeat, expansion of which is responsible for dentatorubral and pallidoluysian atrophy. The protein encoded by this gene interacts with atrophin-1. This encoded protein is a closely related member of the NEDD4-like protein family. This family of proteins are E3 ubiquitin-ligase molecules and regulate key trafficking decisions, including targeting of proteins to proteosomes or lysosomes. This encoded protein contains four tandem WW domains and a HECT (homologous to the E6-associated protein carboxyl terminus) domain. It can act as a transcriptional corepressor of p45/NFE2 and may participate in the regulation of immune responses by modifying Notch-mediated signaling. It is highly similar to the mouse Itch protein, which has been implicated in the regulation and differentiation of erythroid and lymphoid cells.
The E3 ubiquitin ligase Itch regulates sorting nexin 9 through an unconventional substrate recognition domain. Baumann C, et al. FEBS J, 2010 Jul. PMID 20491914.
Cbl-b and itch: key regulators of peripheral T-cell tolerance. Venuprasad K. Cancer Res, 2010 Apr 15. PMID 20395198.
Human ITCH E3 ubiquitin ligase deficiency causes syndromic multisystem autoimmune disease. Lohr NJ, et al. Am J Hum Genet, 2010 Mar 12. PMID 20170897.
Inducible regulatory T cells (iTregs) from recent-onset type 1 diabetes subjects show increased in vitro suppression and higher ITCH levels compared with controls. Glisic S, et al. Cell Tissue Res, 2010 Mar. PMID 20143240.
The ubiquitin ligase itch regulates apoptosis by targeting thioredoxin-interacting protein for ubiquitin-dependent degradation. Zhang P, et al. J Biol Chem, 2010 Mar 19. PMID 20068034.
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