Anti-TRIP12 Polyclonal Antibody for WB, IHC-P, ELISA - Q14669

Core Product Specifications and Parameters

Biological Background: TRIP12 Function and Localization

• The E3 ubiquitin-protein ligase TRIP12 catalyzes substrate ubiquitination and plays a central role in the ubiquitin fusion degradation (UFD) pathway, mediating N-terminal ubiquitination regardless of lysine residue availability. Related references: PMID:19028681

• TRIP12 acts as a key suppressor of RNF168-dependent ubiquitin signaling at DNA damage sites, preventing excessive spreading of 'Lys-63'-linked ubiquitinated histones H2A and H2AX and thereby guarding chromatin integrity. Related references: PMID:22884692 PMID:40419785

• Under normal conditions, TRIP12 mediates ubiquitination and degradation of the lysine-less tumor suppressor p19ARF/ARF (CDKN2A isoform), contributing to p53/TP53 regulation; in cancer cells, compartmental separation prevents this degradation. Related references: PMID:20208519

• Additional substrates include NAE1 and SMARCE1, whose ubiquitination by TRIP12 targets them for proteasomal turnover. Related references: PMID:18627766

• Interaction partners such as MYC, TRADD, and SMARCC1 can disrupt TRIP12 binding to target proteins, providing an extra layer of regulatory control over substrate degradation. Related references: PMID:20829358

• TRIP12 also ubiquitinates ASXL1 upon binding to N6-methyladenosine-methylated DNA, leading to ASXL1 degradation and subsequent inactivation of the PR-DUB complex. Related references: PMID:30982744

• TRIP12 is predominantly localized to the nucleoplasm, where it executes its nuclear functions in DNA repair and protein quality control.

• The protein is subject to post-translational modifications including acetylation and phosphorylation, and belongs to the HECT-type E3 ubiquitin transferase family; mutations in TRIP12 are associated with autism spectrum disorder and intellectual disability.

Experimental Guidance and Technical Tips

• The immunogen corresponds to the N-terminal region (aa 1-240) of human TRIP12, making the antibody potentially suitable for detecting both full-length protein and N-terminal isoforms.
• For western blot, a predominant band at approximately 220 kDa is expected; consider using gradient gels and prolonged transfer times due to the large molecular weight.
• In immunohistochemistry (paraffin-embedded sections), antigen retrieval conditions and primary antibody dilution should be optimized empirically; appropriate controls are essential to confirm nuclear staining.
• ELISA applications may benefit from careful titration of both capture and detection antibodies.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio is a one-stop partner for IVD raw-material sourcing, providing validated antibody pairs, optimized polyclonal antibodies, and bulk ancillary reagents. For investigators exploring the ubiquitin-proteasome pathway or DNA damage response, this anti-TRIP12 antibody supports the development of robust diagnostic and research assays. Our integrated platform bridges the gap from concept to clinic, offering technical consultation and rare target sourcing to streamline your workflow.