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).1) 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.
Immunogen
ITCH antibody was raised against a 15 amino acid peptide near the amino terminus of human ITCH . The immunogen is located within amino acids 40 - 90 of ITCH.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WB
ITCH antibody can be used for detection of ITCH by Western blot at 1 - 2 μg/ml.
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.