Rabbit Polyclonal TRIM8 antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human TRIM8 aa 1-250.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 78.99% PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
WB | IHC-P | |
---|---|---|
Human | Tested | Tested |
Mouse | Predicted | Predicted |
Rat | Predicted | Predicted |
Chicken | Predicted | Predicted |
Cow | Predicted | Predicted |
Xenopus laevis | Predicted | Predicted |
Xenopus tropicalis | Predicted | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/500.00000 - 1/3000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Rat, Chicken, Cow, Xenopus laevis, Xenopus tropicalis | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Rat, Chicken, Cow, Xenopus laevis, Xenopus tropicalis | Dilution info - | Notes - |
E3 ubiquitin-protein ligase that participates in multiple biological processes including cell survival, differentiation, apoptosis, and in particular, the innate immune response (PubMed:27981609, PubMed:28747347). Participates in the activation of interferon-gamma signaling by promoting proteasomal degradation of the repressor SOCS1 (PubMed:12163497). Plays a positive role in the TNFalpha and IL-1beta signaling pathways. Mechanistically, induces the 'Lys-63'-linked polyubiquitination of MAP3K7/TAK1 component leading to the activation of NF-kappa-B (PubMed:22084099, PubMed:23152791, PubMed:27981609, PubMed:34871740). Modulates also STAT3 activity through negative regulation of PIAS3, either by degradation of PIAS3 through the ubiquitin-proteasome pathway or exclusion of PIAS3 from the nucleus (PubMed:20516148). Negatively regulates TLR3/4-mediated innate immune response by catalyzing 'Lys-6'- and 'Lys-33'-linked polyubiquitination of TICAM1 and thereby disrupting the TICAM1-TBK1 interaction (PubMed:28747347).
GERP, RNF27, TRIM8, E3 ubiquitin-protein ligase TRIM8, Glioblastoma-expressed RING finger protein, RING finger protein 27, RING-type E3 ubiquitin transferase TRIM8, Tripartite motif-containing protein 8
Rabbit Polyclonal TRIM8 antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human TRIM8 aa 1-250.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 78.99% PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
TRIM8 also known as Tripartite Motif Containing 8 is an E3 ubiquitin ligase with a known mass of about 61 kDa. This protein facilitates protein degradation via the ubiquitin-proteasome system. It localizes to the nucleus and cytoplasm and is expressed in various tissues such as the brain and immune cells. TRIM8 influences multiple cellular processes by adding ubiquitin chains to specific proteins thereby tagging them for degradation.
TRIM8 is involved in the regulation of signaling pathways and acts as a modulator of cellular functions. TRIM8 participates in the stability and turnover of p53 and STAT3 affecting their transcriptional activities. It also contributes to immune responses by modulating pathways that involve interferon signaling. TRIM8 is not typically part of large protein complexes; its interactions often involve single protein-protein connections.
TRIM8 plays significant roles in immune signaling and apoptosis regulation. It interacts with the NF-kB pathway influencing inflammation and immune responses. Through this pathway TRIM8 impacts the activation of transcriptional activity affecting cellular survival and proliferation. Additionally TRIM8 interacts with proteins like p53 altering its function in the apoptotic pathway thereby influencing cell cycle regulation and survival.
TRIM8 has connections to cancer and neurodegenerative diseases. For cancer abnormalities in TRIM8 expression levels can result in altered p53 activity promoting tumor growth or suppression. In neurodegenerative contexts TRIM8's interaction with STAT3 can affect inflammatory responses linked to diseases like Alzheimer's. These relationships highlight the importance of TRIM8 in both the progression and inhibition of certain pathologies through its interactions with proteins such as p53 and STAT3.
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7.5% SDS PAGE
All lanes: Western blot - Anti-TRIM8 antibody (ab155674) at 1/1000 dilution
All lanes: HepG2 whole cell lysate at 30 µg
Predicted band size: 61 kDa
Immunohistochemical analysis of paraffin-embedded Human Hepatoma tissue, labeling TRIM8 with ab155674 at 1/500 dilution.
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