Analytical Data
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Gene name
TRAIP
- Application
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Alternative Names
TRAIP；RNF206；TRIP；E3 ubiquitin-Protein ligase TRAIP
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BWF2
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Expression Region
1-469aa
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AA Sequence
MPIRALCTICSDFFDHSRDVAAIHCGHTFHLQCLIQWFETAPSRTCPQCRIQVGKRTIINKLFFDLAQEEENVLDAEFLKNELDNVRAQLSQKDKEKRDSQVIIDTLRDTLEERNATVVSLQQALGKAEMLCSTLKKQMKYLEQQQDETKQAQEEARRLRSKMKTMEQIELLLQSQRPEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKASGEVADKLRKDLFSSRSKLQTVYSELDQAKLELKSAQKDLQSADKEIMSLKKKLTMLQETLNLPPVASETVDRLVLESPAPVEVNLKLRRPSFRDDIDLNATFDVDTPPARPSSSQHGYYEKLCLEKSHSPIQDVPKKICKGPRKESQLSLGGQSCAGEPDEELVGAFPIFVRNAILGQKQPKRPRSESSCSKDVVRTGFDGLGGRTKFIQPTDTVMIRPLPVKPKTKVKQRVRVKTVPSLFQAKLDTFLWS
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Molecular Weight
58.8 kDa
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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
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Protein Description
TRAIP (TRAF-interacting protein) is an important protein involved in various cellular processes, including DNA damage response, cell cycle regulation, and apoptosis. Research on TRAIP protein has gained significant attention due to its role in maintaining genomic stability and its potential implications in cancer biology. TRAIP is known to function as an E3 ubiquitin ligase, which facilitates the attachment of ubiquitin molecules to target proteins, thereby regulating their degradation or activity. Dysregulation of TRAIP has been associated with several cancers, including breast and colorectal cancers, highlighting its potential as a biomarker or therapeutic target. The study of TRAIP's structure and function at the molecular level is crucial for understanding its role in tumorigenesis and therapeutic resistance. Recent advancements in protein engineering and structural biology have enabled researchers to characterize TRAIP more comprehensively, paving the way for innovative strategies to modulate its activity. By elucidating the mechanisms underlying TRAIP's function, scientists aim to develop targeted therapies that may enhance treatment efficacy and overcome resistance in cancer patients. Understanding TRAIP’s role in cellular signaling pathways and its interactions with other proteins could provide insights into novel cancer treatment approaches and the design of small molecule inhibitors that could selectively modulate its function. Hence, ongoing research into TRAIP offers promising avenues for cancer therapy and emphasizes the need for a deeper exploration of its biological significance and therapeutic potential.
