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AB111580

Anti-TRIM41 antibody

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(4 Publications)

Rabbit Polyclonal TRIM41 antibody. Suitable for WB, ICC/IF and reacts with Human samples. Cited in 4 publications. Immunogen corresponding to Recombinant Fragment Protein within Human TRIM41 aa 250 to C-terminus.

View Alternative Names

RINCK, TRIM41, E3 ubiquitin-protein ligase TRIM41, RING finger-interacting protein with C kinase, Tripartite motif-containing protein 41

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-TRIM41 antibody (AB111580)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-TRIM41 antibody (AB111580)

ab111580 at 1/200 dilution staining TRIM41 in Paraformaldehyde-fixed HeLa cells by Immunofluorescence. Lower image shows cells co-stained with Hoechst 33342.

Western blot - Anti-TRIM41 antibody (AB111580)
  • WB

Unknown

Western blot - Anti-TRIM41 antibody (AB111580)

7.5% SDS-PAGE.

All lanes:

Western blot - Anti-TRIM41 antibody (ab111580) at 1/1000 dilution

All lanes:

HeLa whole cell lysate at 30 µg

Predicted band size: 72 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, ICC/IF

applications

Immunogen

Recombinant Fragment Protein within Human TRIM41 aa 250 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q8WV44

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

TRIM41 also known as RING finger protein 3 functions as an E3 ubiquitin ligase with a mass of approximately 55 kDa. It interacts with the ubiquitin-proteasome system to tag specific proteins for degradation by attaching ubiquitin molecules. TRIM41 co-exists in the cytoplasm and nucleus of various cell types. This protein exhibits significant expression in tissues such as the liver heart and kidney pointing to its versatile roles in cellular environments.
Biological function summary

TRIM41 contributes to regulating protein turnover and homeostasis within cells. It forms part of a ubiquitin ligase complex which actively recognizes and degrades targeted proteins. This regulation ensures the balance of proteins involved in processes such as cell cycle progression and signal transduction. The protein interacts with other cellular mechanisms to facilitate appropriate cellular responses to stress or changes in the extracellular environment.

Pathways

The role of TRIM41 extends to influencing processes such as the NF-kB signaling pathway and the IRF3 pathway. The NF-kB pathway involves inflammation and immune response while TRIM41 may also modulate the IRF3 pathway which is essential in innate antiviral defense mechanisms. Additionally TRIM41 interacts with proteins like TRAF3 and TRAF6 playing a role in downstream signaling events essential for cellular regulation and protection against pathogens.

TRIM41 becomes particularly relevant in the context of cancer and inflammatory diseases. Abnormal TRIM41 function associates with the development of some cancers where altered protein degradation disrupts normal cell cycle regulation. Inflammatory disorders may also involve TRIM41 due to its role in pathways mediating immune responses. The protein connects with other proteins such as p53 in cancer and NF-kB components in inflammation highlighting its contributions to pathophysiological states.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

E3 ligase that plays essential roles in innate antiviral response (PubMed : 28169297, PubMed : 29760876, PubMed : 29899090, PubMed : 31979016). Directly binds to influenza A virus or vesicular stomatitis virus nucleoproteins and targets them for ubiquitination and proteasomal degradation, thereby limiting viral infections (PubMed : 28169297, PubMed : 29899090, PubMed : 31979016). Activates the innate antiviral response by catalyzing monoubiquitination of CGAS, thereby activating CGAS (PubMed : 29760876). Also involved in innate antiviral response by mediating 'Lys-63'-linked polyubiquitylation of BCL10 which in turn hubs NEMO for activation of NF-kappa-B and IRF3 pathways (By similarity). Catalyzes the ubiquitin-mediated degradation of other substrates including protein kinase C, ZSCAN21 or TOP3B suggesting additional roles besides its function in immune response (PubMed : 17893151, PubMed : 33378676).
See full target information TRIM41

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

PloS one 19:e0313939 PubMed39585848

2024

Validation of the biological function and prognostic significance of AURKA in neuroblastoma.

Applications

Unspecified application

Species

Unspecified reactive species

Jing Chu

Nature communications 14:7524 PubMed37980342

2023

The TDRD3-USP9X complex and MIB1 regulate TOP3B homeostasis and prevent deleterious TOP3B cleavage complexes.

Applications

Unspecified application

Species

Unspecified reactive species

Sourav Saha,Shar-Yin Naomi Huang,Xi Yang,Liton Kumar Saha,Yilun Sun,Prashant Khandagale,Lisa M Jenkins,Yves Pommier

Nature communications 14:1925 PubMed37024461

2023

Replication-associated formation and repair of human topoisomerase IIIα cleavage complexes.

Applications

Unspecified application

Species

Unspecified reactive species

Liton Kumar Saha,Sourav Saha,Xi Yang,Shar-Yin Naomi Huang,Yilun Sun,Ukhyun Jo,Yves Pommier

Molecular cell 81:599-613.e8 PubMed33373584

2020

Structural analysis of RIG-I-like receptors reveals ancient rules of engagement between diverse RNA helicases and TRIM ubiquitin ligases.

Applications

Unspecified application

Species

Unspecified reactive species

Kazuki Kato,Sadeem Ahmad,Zixiang Zhu,Janet M Young,Xin Mu,Sehoon Park,Harmit S Malik,Sun Hur
View all publications

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