TRIM21 Human Biotin
Greater than 80% as determined by SDS-PAGE.
Description
TRIM21 Human Recombinant, Biotin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 52kDa.
TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
TRIM21, a protein belonging to the tripartite motif (TRIM) family, is characterized by the presence of a TRIM motif. This motif comprises three zinc-binding domains: a RING domain, a B-box type 1, and a B-box type 2, along with a coiled-coil region. The 52 kDa Ro protein is an integral component of the RoSSA ribonucleoprotein, which consists of a single polypeptide and one out of four potential small RNA molecules. The RoSSA particle is found in both the cytoplasm and the nucleus of cells. In individuals with Sjogren syndrome and systemic lupus erythematosus, Ro/SSA exhibits interaction with autoantigens. Ribonucleoprotein particles, in general, are composed of a single polypeptide and one of four specific small RNA molecules. Although present in all studied mammalian cells, the RoSSA's function remains unknown. Notably, at least two isoforms are found in nucleated cells and red blood cells, indicating tissue-specific variations in Ro/SSA proteins.
Recombinantly produced in SF9 cells, TRIM21 Human Recombinant, Biotin is a glycosylated polypeptide chain with an estimated molecular weight of 52kDa. The protein is expressed with a 6x His tag positioned at the N-terminus and is purified using proprietary chromatographic techniques.
The product is a clear solution that has been sterilized by filtration.
The provided TRIM21 solution is formulated in a buffer containing 20mM HEPES at a pH of 7.6, 0.01mM EDTA, and 0.02% SDS.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. It's important to avoid repeated freeze-thaw cycles to maintain product integrity.
The purity of the product is determined to be greater than 80% using SDS-PAGE analysis.
The product exhibits the following immunological functions: 1. It can bind to human autoantibodies of the IgG type. 2. It can be utilized in functional Streptavidin-based ELISA tests for the analysis of both positive and negative samples.
Product Science Overview
Tripartite Motif Containing 21 (TRIM21), also known as RO52, is a protein encoded by the TRIM21 gene in humans. It is a member of the tripartite motif (TRIM) family, which is characterized by the presence of three zinc-binding domains: a RING finger domain, a B-box type 1, and a B-box type 2, along with a coiled-coil region . TRIM21 is an E3 ubiquitin-protein ligase and plays a crucial role in the immune system by acting as an intracellular antibody receptor .
TRIM21 is involved in the intracellular antibody-mediated proteolysis pathway. It recognizes and binds to the Fc domain of immunoglobulins such as IgG, IgA, and IgM on antibody-marked non-enveloped virions that have infected the cell . This binding triggers the ubiquitination and subsequent proteasomal degradation of the virions, providing a last line of defense against invading viruses . Additionally, TRIM21 is implicated in various biological processes, including the regulation of type I interferon production, protein ubiquitination, and the innate immune response .
TRIM21 is associated with autoimmune diseases such as Sjogren’s syndrome and systemic lupus erythematosus (SLE). Autoantibodies targeting TRIM21 are commonly found in patients with these conditions . The presence of these autoantibodies can serve as a diagnostic marker for these autoimmune diseases.
Human recombinant TRIM21, biotinylated, is produced using recombinant DNA technology. It is expressed in various host systems, such as E. coli or insect cells, and purified using chromatographic techniques . The biotinylation of TRIM21 allows for its use in various biochemical assays, including enzyme-linked immunosorbent assays (ELISAs) and Western blotting, where it can be detected with high sensitivity and specificity .
