Analytical Data
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Gene name
ITCH
- Application
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Alternative Names
ITCH；E3 ubiquitin-Protein ligase Itchy homolog
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Species
MOUSE
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Source
E. coli
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Tag
His Tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8C863
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Expression Region
562-864 aa
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AA Sequence
IMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECGLEMYFSVDKEILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRHYTRTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVGKENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE
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Molecular Weight
34kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Identification
Protein Description
ITCH is an E3 ubiquitin ligase that plays a critical role in the regulation of cellular processes, including apoptosis, immune response, and signal transduction. Its unique function lies in mediating the ubiquitination of target proteins, thereby influencing their stability and activity. Dysregulation of ITCH has been implicated in various diseases, including cancer and autoimmune disorders. The recombinant expression of ITCH protein allows for detailed studies of its biochemical properties and interactions with other cellular proteins. By utilizing techniques such as site-directed mutagenesis and co-immunoprecipitation, researchers can investigate the functional consequences of ITCH-mediated ubiquitination on key signaling pathways. Additionally, understanding the structural basis of ITCH's activity may facilitate the development of novel therapeutic strategies aimed at restoring its function or inhibiting its overactivity in pathological conditions. As interest in protein ubiquitination grows, the characterization of ITCH as a significant regulator in this field underscores its potential as a target for drug discovery and therapeutic intervention. This research not only aims to deepen the understanding of ITCH’s role in cellular regulation but also contributes to the broader field of proteomics and cellular signaling.
