Analytical Data
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Gene name
TRIM31
- Application
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Alternative Names
TRIM31; C6orf13; RNF; E3 ubiquitin-Protein ligase TRIM31; EC 2.3.2.27; RING-type E3 ubiquitin transferase TRIM31; Tripartite motif-containing Protein 31
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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
Q9BZY9
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Expression Region
1-425 aa
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AA Sequence
MASGQFVNKL QEEVICPICL DILQKPVTID CGHNFCLKCI TQIGETSCGF FKCPLCKTSV RKNAIRFNSL LRNLVEKIQA LQASEVQSKR KEATCPRHQE MFHYFCEDDG KFLCFVCRES KDHKSHNVSL IEEAAQNYQG QIQEQIQVLQ QKEKETVQVK AQGVHRVDVF TDQVEHEKQR ILTEFELLHQ VLEEEKNFLL SRIYWLGHEG TEAGKHYVAS TEPQLNDLKK LVDSLKTKQN MPPRQLLEDI KVVLCRSEEF QFLNPTPVPL ELEKKLSEAK SRHDSITGSL KKFKDQLQAD RKKDENRFFK SMNKNDMKSW GLLQKNNHKM NKTSEPGSSS AGGRTTSGPP NHHSSAPSHS LFRASSAGKV TFPVCLLASY DEISGQGASS QDTKTFDVAL SEELHAALSE WLTAIRAWFC EVPSS
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Molecular Weight
48.2 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
TRIM31, a member of the TRIM (tripartite motif-containing) protein family, has garnered significant attention in recent years due to its diverse roles in cellular processes and disease mechanisms. TRIM proteins are characterized by their tripartite structure, which typically includes a RING domain, one or two B-box motifs, and a coiled-coil domain, allowing them to function in ubiquitination, signal transduction, and transcriptional regulation. TRIM31, in particular, has been implicated in the regulation of immune responses, inflammation, and tumorigenesis. Studies suggest that TRIM31 can modulate the activity of various signaling pathways, including the NF-kB and MAPK pathways, which are crucial for immune and inflammatory responses. Additionally, aberrant expression of TRIM31 has been linked to several cancers, making it a potential biomarker and therapeutic target. Research on TRIM31 has focused on elucidating its molecular mechanisms and interactions within the cell, particularly in the context of autoimmune diseases and cancer. Understanding the functional roles and regulatory networks of TRIM31 will not only enhance our knowledge of its biological significance but may also open new avenues for developing targeted therapies against diseases associated with its dysregulation. Overall, the study of TRIM31 represents a promising frontier in the exploration of protein functional dynamics and their implications in human health and disease.
