Recombinant human ITCH/AIP4 protein (ab190328)

Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      MSDSGSQLGSMGSLTMKSQLQITVISAKLKENKKNWFGPSPYVEVTVDGQ SKKTEKCNNT NSPKWKQPLTVIVTPVSKLHFRVWSHQTLKSDVLLGTA ALDIYETLKSNNMKLEEVVVTL QLGGDKEPTETIGDLSICLDGLQLES EVVTNGETTCSESASQNDDGSRSKDETRVSTNGS DDPEDAGAGENRRV SGNNSPSLSNGGFKPSRPPRPSRPPPPTPRRPASVNGSPSATSESD GS STGSLPPTNTNTNTSEGATSGLIIPLTISGGSGPRPLNPVTQAPLPPGWE QRVDQHGR VYYVDHVEKRTTWDRPEPLPPGWERRVDNMGRIYYVDHFT RTTTWQRPTLESVRNYEQWQ LQRSQLQGAMQQFNQRFIYGNQDLFATS QSKEFDPLGPLPPGWEKRTDSNGRVYFVNHNT RITQWEDPRSQGQLNE KPLPEGWEMRFTVDGIPYFVDHNRRTTTYIDPRTGKSALDNGPQ IAYV RDFKAKVQYFRFWCQQLAMPQHIKITVTRKTLFEDSFQQIMSFSPQDLRR RLWVIF PGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQ INPASYINPDHLKYFRFI GRFIAMALFHGKFIDTGFSLPFYKRILNKP VGLKDLESIDPEFYNSLIWVKENNIEECDL EMYFSVDKEILGEIKSHD LKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGF NEILPQ QYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRHYARTSKQIMWFWQFVK EIDN EKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVGKENWL PRSHTCFNRLDLPPYK SYEQLKEKLLFAIEETEGFGQE
    • Molecular weight
      99 kDa
    • Amino acids
      1 to 862

Associated products

Specifications

Our Abpromise guarantee covers the use of ab190328 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activity

    This untagged, ITCH/AIP4 isoform 2 recombinant protein demonstrates strong autoubiquitination activity in vitro. Typical enzyme concentration to support conjugation in vitro is 0.1-0.5 µM depending on experimental conditions.

  • Applications

    SDS-PAGE

    Functional Studies

  • Purity
    >90% by SDS-PAGE.

  • Form
    Liquid
  • Additional notes

    Recombinant Human ITCH/AIP4 is a HECT domain Ubiquitin ligase (E3) that functions downstream of a Ubiquitinactivating (E1) enzyme and a Ubiquitinconjugating (E2) enzyme to conjugate Ubiquitin to substrate proteins. Reaction conditions will need to be optimized for each specific application.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.

    pH: 7.5
    Constituents: 1.19% HEPES, 0.88% Sodium chloride, 10% Glycerol, 0.58% TCEP

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • ADMFD
    • AIF4
    • AIP4
    • Atrophin 1 interacting protein 4
    • Atrophin-1-interacting protein 4
    • dJ468O1.1
    • dJ468O1.1 (atrophin 1 interacting protein 4 (AIP4))
    • dJ468O1.1 atrophin 1 interacting protein 4 AIP4
    • E3 ubiquitin protein ligase Itchy homolog
    • E3 ubiquitin-protein ligase Itchy homolog
    • EC 6.3.2
    • Itch
    • ITCH_HUMAN
    • Itchy E3 ubiquitin protein ligase
    • Itchy E3 ubiquitin protein ligase homolog
    • Itchy E3 ubiquitin protein ligase homolog mouse
    • Itchy E3 ubiquitin protein ligase, mouse, homolog of
    • Itchy homolog E3 ubiquitin protein ligase
    • Itchy mouse homolog E3 ubiquitin protein ligase
    • NAPP1
    • NFE2 associated polypeptide 1
    • NFE2-associated polypeptide 1
    • Ubiquitin protein ligase ITCH
    see all
  • 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 proteosomal 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 proteosomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteosomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteosomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination.
  • Tissue specificity
    Widely expressed.
  • Pathway
    Protein modification; protein ubiquitination.
  • Involvement in disease
    Defects in ITCH are the cause of syndromic multisystem autoimmune disease (SMAD) [MIM:613385]. SMAD is characterized by organomegaly, failure to thrive, developmental delay, dysmorphic features and autoimmune inflammatory cell infiltration of the lungs, liver and gut.
  • Sequence similarities
    Contains 1 C2 domain.
    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.
    Contains 4 WW domains.
  • Post-translational
    modifications
    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.
    Ubiquitinated; autopolyubiquitination with 'Lys-63' linkages which does not lead to protein degradation.
  • Cellular localization
    Cell membrane. Cytoplasm. Nucleus. Associates with endocytic vesicles. May be recruited to exosomes by NDFIP1.
  • Information by UniProt

References

ab190328 has not yet been referenced specifically in any publications.

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