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Recombinant Mouse E3 ubiquitin-protein ligase Itchy (Itch), partial

Recombinant Mouse E3 ubiquitin-protein ligase Itchy (Itch), partial

Code	CSB-YP806500MO
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP806500MO
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP806500MO-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP806500MO
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP806500MO
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

Itch

Uniprot No.

Q8C863

Alternative Names

Itch; E3 ubiquitin-protein ligase Itchy; EC 2.3.2.26; HECT-type E3 ubiquitin transferase Itchy homolog

Species

Mus musculus (Mouse)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

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. 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 involved in immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Mediates JUN ubiquitination and degradation. Mediates JUNB ubiquitination and degradation. Critical regulator of type 2 helper T (Th2) cell cytokine production by inducing JUNB ubiquitination and degradation. Involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Following ligand stimulation, regulates sorting of Wnt receptor FZD4 to the degradative endocytic pathway probably by modulating PI42KA activity. Ubiquitinates PI4K2A and negatively regulates its catalytic activity. 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. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination. Ubiquitinates SNX9. Ubiquitinates MAP3K7 through 'Lys-48'-linked conjugation. 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. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1.

Gene References into Functions

beta-Arrestin2 increases the Itch-mediated ubiquitylation of SuFu. PMID: 29515120
findings show that the WW domains proceeding the catalytic HECT domain play an inhibitory role by binding directly to HECT in Itch; study provides a new mechanism governing the regulation of Itch PMID: 28747490
this study identified a previously unknown role for Itch in regulating IL-17-mediated colonic inflammation and carcinogenesis PMID: 27322655
Itch monoubiquitinates SMN and monoubiquitination of SMN plays an important role in regulating its cellular localization. PMID: 26908624
ITCH targets TXNIP for ubiquitin-proteasome degradation in cardiomyocytes and ameliorates reactive oxygen species-induced cardiotoxicity through the thioredoxin system. PMID: 26796253
CUL4B links two distinct spermatogenetic processes to a single E3 ligase, highlighting the significance of ubiquitin modification during spermatogenesis. PMID: 26846852
The Itch plays a role in epidermal homeostasis and remodelling and this feature does not seem to depend on immunological alterations. PMID: 26361888
Impaired ITCH results in heightened TNF signaling. ITCH-/- mouse's spontaneous lung inflammation and subsequent death can be delayed when TNF signaling is genetically deleted. PMID: 26190110
ITCH modulates SIRT6 and SREBP2 to influence lipid metabolism and atherosclerosis in ApoE null mice PMID: 25777360
Upregulated microRNA-214 enhances cardiac injury by targeting ITCH during coxsackievirus infection. PMID: 25815880
In the absence of Ndfip1, the Nedd4 family member Itch can bind an E2 but cannot accept ubiquitin onto its catalytic cysteine. PMID: 26245901
The E3 ubiquitin ligase Itch inhibits p38alpha signaling and skin inflammation through the ubiquitylation of Tab1. PMID: 25714464
Ndfip1 regulates itch ligase activity and airway inflammation via UbcH7. PMID: 25632008
Itch acts as an essential positive regulator in the differentiation of follicular T cells. PMID: 24859451
The expression of Th2 cytokines by Treg cells was increased in the absence of Itch. Fate mapping revealed that a fraction of Treg cells lost Foxp3 expression independently of Itch. PMID: 24135136
identify Itch as a regulator of Oct4 stability and transcriptional activity, establishing a functional link between an E3 ligase and the regulation of pluripotency PMID: 23255053
Itch interacts with the deubiquitinating enzyme and is required for deubiquitination of TRAF6, thus limiting RANKL-induced osteoclast formation PMID: 23782702
Itch directly associates with and ubiquitinates PI4KIIalpha, and both proteins colocalize on endosomes containing Wnt-activated frizzled 4 (Fz4) receptor PMID: 23146885
we have identified an Itch-Cyld-mediated regulatory mechanism in innate inflammatory cells. PMID: 22057290
Itch deficiency in hematopoietic stem cells is associated with increased signaling by the transcription factor Notch1. PMID: 21478879
E3 ubiquitin ligase Idol (inducible degrader of the Ldlr)expression is required for the ability of liver x receptor to stimulate Ldlr protein degradation. PMID: 21343340
gene deletion of both Cbl-b and Itch leads to augmented T cell activation and spontaneous autoimmunity PMID: 20637659
CTLA-4 mediates signals via the activation of the ubiquitin ligase Itch PMID: 20417562
Cbl-b and itch are key regulators of peripheral T-cell tolerance [review] PMID: 20395198
Data show that activation of TNF-alpha signaling induced the association of TGIF with Itch/AIP4, resulting in increased accessibility of cFlip(L) for association and ubiquitination by Itch/AIP4. PMID: 20064471
These results suggest that Itch can facilitate MoMLV release in an L domain-independent manner via a mechanism that requires the host budding machinery and involves Gag ubiquitination. PMID: 19864377
Cbl-b knockout mice are available. Negative regulation of immune responses by three new E3 ubiquitin-protein ligases, Cbl, Cbl-b, & Itch is mediated by TCR, PI3-K, Notch and Lck. PMID: 11826757
downmodulated LMP2A activity in B-cell signaling PMID: 12692257
Loss of Itch E3 ligase in mouse embryonic fibroblasts causes reduced susceptibility of TGF-beta-induced cell growth arrest and decreased phosphorylation of Smad2 Itch-/- MEFs. PMID: 15350225
activation of the Jun amino-terminal kinase (JNK) mitogen-activated protein kinase cascade after T cell stimulation accelerated degradation of c-Jun and JunB through phosphorylation-dependent activation of the E3 ligase Itch PMID: 15358865
Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain PMID: 15971201
This study suggests that MEKK1-JNK signaling regulates Itch E3 ligase-mediated tolerogenic process in Th2 cells. These findings have therapeutic implications for allergic diseases PMID: 16557301
results identify a synapse-associated E3 ubiquitin ligase as an important regulator of MuSK signaling PMID: 17576800
Inhibition of Itch by Nedd4-binding partner 1 (N4BP1) results in the stabilization of crucial cell death regulators such as p73 alpha and c-Jun. PMID: 17592138
These data indicate that disruption of an E3 ubiquitin ligase in alphabeta T cells can subvert a B-cell subpopulation, which normally functions to control particular microbial pathogens in a T-independent manner, to contribute to autoimmunity. PMID: 18256323
AIP4/Itch regulates Notch receptor degradation in the absence of ligand PMID: 18628966
Both Itch and the MEKK1 kinase domain are important for Il4 and Il6 cytokine gene expression under Th2 conditions. PMID: 19710465
MKK4 is negatively regulated through a feedback loop involving the E3 ubiquitin ligase Itch, which has a fundamental role in the mechanism that controls MKK4 protein levels. PMID: 19737936
PCBP2-AIP4(Itch) axis defines a new PCBP2-AIP4 axis defines a new signaling cascade for MAVS degradation and 'fine tuning' of antiviral innate immunity. PMID: 19881509

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Involvement in disease

Defects in Itch are the cause of the itchy phenotype which is an inflammatory and immunological condition characterized by inflammation in the lung and stomach, hyperplasia in lymphoid and hematopoietic cells and constant itching in the skin.

Subcellular 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.

Tissue Specificity

Detected in uterus (at protein level). Widely expressed.

Database Links

KEGG: mmu:16396

STRING: 10090.ENSMUSP00000029126

UniGene: Mm.208286

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