Anti-TRIM13 antibody - N-terminal
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(2 Publications)
Mouse Polyclonal TRIM13 antibody. N-terminal. Suitable for WB and reacts with Recombinant fragment - Human, Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human TRIM13 aa 1-100.
View Alternative Names
LEU5, RFP2, RNF77, TRIM13, E3 ubiquitin-protein ligase TRIM13, B-cell chronic lymphocytic leukemia tumor suppressor Leu5, Leukemia-associated protein 5, Putative tumor suppressor RFP2, RING finger protein 77, RING-type E3 ubiquitin transferase TRIM13, Ret finger protein 2, Tripartite motif-containing protein 13
- WB
Supplier Data
Western blot - Anti-TRIM13 antibody - N-terminal (AB194477)
All lanes:
Western blot - Anti-TRIM13 antibody - N-terminal (ab194477) at 1/500 dilution
All lanes:
HeLa cell lysate at 50 µg
Predicted band size: 47 kDa
true
- WB
Supplier Data
Western blot - Anti-TRIM13 antibody - N-terminal (AB194477)
Predicted MWt of immunogen : 37.11 KDa.
All lanes:
Western blot - Anti-TRIM13 antibody - N-terminal (ab194477) at 1/1000 dilution
All lanes:
recombinant immunogen at 0.2 µg
Predicted band size: 47 kDa
true
Reactivity data
Properties and storage information
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
This protein is important for maintaining cellular homeostasis by regulating protein turnover and quality control. TRIM13 is involved in the endoplasmic reticulum-associated degradation (ERAD) pathway where it facilitates the removal of misfolded proteins. Additionally it interacts with other molecules to form complexes that modulate autophagy a process vital for cellular cleaning and response to stress.
Pathways
Ubiquitination processes and quality control systems incorporate TRIM13 into the intricacies of the ERAD and autophagy pathways. It coordinates with proteins like p62 and Beclin1 which are important for autophagy regulation. In the ERAD pathway TRIM13 functions alongside components such as Derlin-1 helping to identify and direct aberrant proteins toward degradation. These interactions balance protein synthesis and degradation essential for cellular stress responses and survival.
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Target data
Publications (2)
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iScience 28:113101 PubMed40746991
2025
Applications
Unspecified application
Species
Unspecified reactive species
Science advances 8:eabm0478 PubMed35353581
2022
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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