Analytical Data
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Gene name
TRIM21
- Application
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Alternative Names
TRIM21；RNF81；RO52；SSA1；E3 ubiquitin-Protein ligase TRIM21
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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
P19474
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Expression Region
1-475aa
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AA Sequence
MASAARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEISQEAREGTQGERCAVHGERLHLFCEKDGKALCWVCAQSRKHRDHAMVPLEEAAQEYQEKLQVALGELRRKQELAEKLEVEIAIKRADWKKTVETQKSRIHAEFVQQKNFLVEEEQRQLQELEKDEREQLRILGEKEAKLAQQSQALQELISELDRRCHSSALELLQEVIIVLERSESWNLKDLDITSPELRSVCHVPGLKKMLRTCAVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTLCPLNIGSQGSTDY
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Molecular Weight
57.7 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
Related Products
Protein Description
TRIM21, also known as Ro52, is a member of the TRIM (Tripartite Motif) family of proteins recognized for their roles in various cellular processes, including immune response, apoptosis, and the regulation of protein degradation via the ubiquitin-proteasome system. It has gained significant attention in recent years due to its unique ability to act as an intracellular antibody that can recognize and neutralize viral particles in the cytoplasm. This function is particularly critical in the context of viral infections, where TRIM21 facilitates the targeted degradation of viral proteins, thus playing a pivotal role in the innate immune response. Furthermore, TRIM21's involvement in autoimmune diseases, particularly in connection with anti-Ro antibodies found in systemic lupus erythematosus (SLE) patients, highlights its dual role as both a protective and potentially pathogenic factor. The recombinant expression of TRIM21 has become a focus of research to better understand its structure-function relationship and potential therapeutic applications. By producing TRIM21 as a recombinant protein, researchers aim to dissect its mechanisms of action in immune modulation and its potential as a target for novel therapeutic strategies against viral infections and autoimmune disorders. The study of TRIM21 continues to reveal intriguing insights into the intersection of immunity and pathology, advancing our understanding of how this multifunctional protein can be harnessed for clinical benefits.
