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AB128814

Anti-TRIM11 antibody

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(1 Publication)

Goat Polyclonal TRIM11 antibody. Suitable for WB and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human TRIM11 aa 200-300.

View Alternative Names

RNF92, TRIM11, E3 ubiquitin-protein ligase TRIM11, Protein BIA1, RING finger protein 92, Tripartite motif-containing protein 11

1 Images
Western blot - Anti-TRIM11 antibody (AB128814)
  • WB

Unknown

Western blot - Anti-TRIM11 antibody (AB128814)

All lanes:

Western blot - Anti-TRIM11 antibody (ab128814) at 0.3 µg/mL

All lanes:

Human spleen lysate in RIPA buffer at 35 µg

Predicted band size: 53 kDa

true

Exposure time: 1hr

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Synthetic Peptide within Human TRIM11 aa 200-300. The exact immunogen used to generate this antibody is proprietary information.

Q96F44

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "0.3-1 µg/mL", "WB-species-notes": "<p>1 hour primary incubation is recommended for this product.</p>" }, "Cow": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.3 Preservative: 0.02% Sodium azide Constituents: 99% Tris buffered saline, 0.5% 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.

TRIM11 also known as Tripartite Motif Containing 11 is a protein with a mass of approximately 54 kDa. It functions as an E3 ubiquitin ligase facilitating the transfer of ubiquitin from E2 enzymes to target proteins which signals these targets for degradation by the proteasome. This protein is expressed in various tissues with higher levels found in the brain. It plays a role in controlling protein homeostasis and impacts several cellular processes.
Biological function summary

TRIM11 influences neuronal development and survival. It is involved in regulating the degradation of specific substrates important for neuronal functions. TRIM11 is not part of a well-defined complex but it interacts with key proteins that modulate cellular stress responses. This interaction helps in maintaining cellular balance especially under conditions that challenge cellular homeostasis.

Pathways

Several important cellular functions involve TRIM11 notably the ubiquitin-proteasome pathway. TRIM11 interacts with proteins like HIF1α and impacts the hypoxia pathway. By regulating the availability of certain transcription factors TRIM11 can influence how cells respond to low oxygen conditions. Additionally through its ubiquitin ligase activity TRIM11 plays a part in modulating apoptosis highlighting its role in cell survival pathways.

TRIM11 has been associated with neurodegenerative disorders and cancer. In the context of neurodegenerative diseases abnormal regulation of TRIM11 can disrupt normal protein homeostasis in neurons contributing to conditions like Alzheimer's disease. Additionally TRIM11 may impact cancer progression by interacting with and modulating the stability of tumor suppressor proteins such as p53. This link emphasizes its potential as a target for therapeutic advancements in these complex diseases.

Product protocols

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

Target data

E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX (By similarity). Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis (By similarity). May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences (By similarity). May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway (By similarity). Mediates MED15 ubiquitination leading to proteasomal degradation (PubMed : 16904669). May contribute to the innate restriction of retroviruses (PubMed : 18248090). Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression (PubMed : 18248090). Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain (PubMed : 18248090). May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle (PubMed : 18248090). Acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2 (PubMed : 27498865). Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes (PubMed : 27498865).
See full target information TRIM11

Publications (1)

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

Molecular medicine reports 16:7752-7758 PubMed28944846

2017

Hedyotis diffusa Willd suppresses metastasis in 5‑fluorouracil‑resistant colorectal cancer cells by regulating the TGF‑β signaling pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Zijun Lai,Zhaokun Yan,Wujin Chen,Jun Peng,Jianyu Feng,Qiongyu Li,Yiyi Jin,Jiumao Lin
View all publications

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