Analytical Data
-
Gene name
TRIM11
- Application
-
Alternative Names
TRIM11；RNF92；E3 ubiquitin-Protein ligase TRIM11
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96F44
-
Expression Region
1-468aa
-
AA Sequence
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ
-
Molecular Weight
58.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Protein Description
TRIM11, a member of the Tripartite Motif (TRIM) protein family, has gained attention in recent years due to its potential roles in various cellular processes and its implications in diseases, particularly cancer. TRIM proteins are characterized by a conserved tripartite motif that typically includes a RING finger domain, B-box, and coiled-coil region, allowing them to function as E3 ubiquitin ligases, facilitating protein degradation and regulating various signaling pathways. Research has indicated that TRIM11 participates in the regulation of immune responses, cell proliferation, and apoptosis, positioning it as a critical factor in oncogenesis. Notably, altered expression of TRIM11 has been associated with several types of cancers, suggesting its potential as a biomarker or therapeutic target. The study of TRIM11 recombinant protein is vital for understanding its biochemical properties, interactions with other proteins, and its functional roles in cellular signaling. Investigating the structure-function relationship of TRIM11 can elucidate its mechanisms of action, contribute to our knowledge of tumor biology, and pave the way for new therapeutic strategies in cancer treatment. Furthermore, exploring the modulation of TRIM11 activity may offer insights into the development of novel drugs aimed at combating malignancies where TRIM11 is dysregulated. Overall, the research surrounding TRIM11 recombinant protein is a promising avenue in both basic and applied medical science, fostering a deeper understanding of its implications in human health and disease.
