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ABC926

Sigma-Aldrich

Anti-TRIM11 Antibody

from rabbit, purified by affinity chromatography

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Synonym(s):
E3 ubiquitin-protein ligase TRIM11, Protein BIA1, RING finger protein 92, Tripartite motif-containing protein 11, TRIM11
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

mouse, human

species reactivity (predicted by homology)

canine (based on 100% sequence homology), rhesus macaque (based on 100% sequence homology)

technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... TRIM11(81559)
mouse ... Trim11(94091)

General description

E3 ubiquitin-protein ligase TRIM11 (UniProt Q96F44; also known as Protein BIA1, RING finger protein 92, Tripartite motif-containing 11, Tripartite motif-containing protein 11) is encoded by the TRIM11 (also known as BIA1, RNF92) gene (Gene ID 81559) in human. TRIM11 belongs to a family of more than 70 TRIM/RBCC proteins characterized by their shared tripartite motif structure, also known as the RBCC (RING finger, B-box, and coiled-coil) domain. The B-box and coiled coil regions are believed to participate in protein-protein interactions and formation of macromolecular complexes. TRIM proteins are involved in diverse cellular processes, including cell proliferation, differentiation, oncogenesis, and apoptosis. The presence of a RING domain suggests that TRIM proteins function as E3 ubiquitin ligases. The neuroprotective peptide humanin, activator-recruited cofactor (ARC) 105-kDa component (ARC105), the transcription factors Pax6 and PHOX2B are all known subrates targeted by TRIM11-mediated degradation through the ubiquitin-proteasome system. In addition, TRIM11 is also reported to interfere with the early steps of HIV-1 replication in host cells in a RING domain-dependent manner.

Specificity

This antibody is expected to react with all three spliced isoforms of human TRIM11.

Immunogen

KLH-conjugated linear peptide corresponding to human TRIM11.

Application

Detect TRIM11 using this rabbit polyclonal Anti-TRIM11 Antibody, Cat. No. ABC926, validated for use in Western Blotting and Immunohistochemistry (Paraffin).
Immunohistochemistry Analysis: A 1:50-250 dilution from a representative lot detected TRIM11 in human prostate cancer, human colon cancer, human melanoma, and human kidney tissue.
Research Category
Apoptosis & Cancer
Research Sub Category
Apoptosis - Additional

Quality

Evaluated by Western Blotting in murine macrophage RAW264.7 cell lysate.

Western Blotting Analysis: 1.0 µg/mL of this antibody detected TRIM11 in 10 µg of murine macrophage RAW264.7 cell lysate.

Target description

~53 kDa observed. 52.8 kDa (isoform 1), 43.0 kDa (isoform 2), and 52.6 kDa (isoform 3) calculated.

Physical form

Affinity purified
Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Liang Chen et al.
Nature communications, 9(1), 1223-1223 (2018-03-28)
The proteasome is a complex protease critical for protein quality control and cell regulation, and its dysfunction is associated with cancer and other diseases. However, the mechanisms that control proteasome activity  in normal and malignant cells remain unclear. Here we report
Guixin Zhu et al.
Cell reports, 33(9), 108418-108418 (2020-12-03)
Neurodegenerative diseases are characterized by the formation and propagation of protein aggregates, especially amyloid fibrils. However, what normally suppresses protein misfolding and aggregation in metazoan cells remains incompletely understood. Here, we show that TRIM11, a member of the metazoan tripartite

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