TRAPPC13 antibodies are polyclonal or monoclonal antibodies specifically targeting the TRAPPC13 protein, which is part of the TRAPPIII complex in humans. These antibodies are utilized in techniques such as:
Western blotting (detecting endogenous TRAPPC13 in cell lysates)
Immunofluorescence microscopy (localizing TRAPPC13 to Golgi and ER-associated compartments)
Co-immunoprecipitation (Co-IP) (identifying TRAPPC13 interaction partners like TRAPPC3, TRAPPC4, and Rab1 GTPases)
Functional studies (assessing autophagy flux and Golgi integrity under stress conditions)
Autophagy regulation: TRAPPC13 depletion reduces Rab1a/b GTPase activity, impairing autophagosome formation and flux . Antibody-based assays confirmed that TRAPPC13 knockdown cells exhibit diminished LC3-II accumulation under brefeldin A (BFA) treatment, indicating defective autophagy .
Golgi stress survival: Cells lacking TRAPPC13 show resistance to Golgi-disrupting agents (e.g., BFA, golgicide A) due to preserved ARF1-GBF1 activity and reduced ER stress . Immunofluorescence using TRAPPC13 antibodies revealed less fragmented Golgi structures in knockdown cells during BFA exposure .
TRAPPC13 antibodies identified its interaction with Shigella flexneri, a bacterial pathogen. Depletion of TRAPPC13 increases bacterial infectivity by impairing autophagy-mediated clearance .
In plants, TRAPPC13 interacts with Mesorhizobium amorphae effector protein NopP, as shown by yeast two-hybrid and bimolecular fluorescence complementation (BiFC) assays .
TRAPP complex integrity: TRAPPC13 antibodies confirmed that TRAPPC13 loss does not disrupt core TRAPP complex assembly but reduces Rab1 activation, critical for autophagosome maturation .
ARF1 dependency: Antibody-based ARF-GTP pulldown assays showed TRAPPC13 knockdown maintains ARF1 activity during BFA treatment, enabling secretory pathway preservation .
TRAPPC13 antibodies have proven essential in elucidating: