The SEC11 homologs (e.g., SEC11A, SEC11C) are catalytic subunits of the SPC, which cleaves N-terminal signal peptides from nascent proteins during translocation into the ER lumen . Key functions include:
Signal Peptide Cleavage: Essential for maturation of secretory and membrane proteins .
Quality Control: The SPC, including SEC11C, degrades misfolded membrane proteins to maintain ER proteostasis .
SNARE Regulation: In plants, SEC11 interacts with Qa-SNARE SYP121 to regulate vesicle fusion and SNARE complex recycling .
SEC11 antibodies are polyclonal or monoclonal reagents optimized for applications such as Western blot (WB), ELISA, and immunohistochemistry (IHC). Below is a comparative analysis of commercially available SEC11 antibodies:
The human SPC, including SEC11C, cleaves structurally defective membrane proteins, facilitating their degradation via ER-associated pathways .
Mutations in SEC11 orthologs disrupt signal peptide processing in yeast (Saccharomyces cerevisiae), leading to lethal phenotypes and accumulation of unprocessed proteins .
In Arabidopsis, SEC11 binds the N-terminal domain of SYP121, a plasma membrane Qa-SNARE, to regulate secretory traffic .
SEC11 competes with SNAP33 and VAMP721 for SYP121 binding, suggesting a "handshake" mechanism to modulate SNARE complex assembly .
Western Blot: Detects SEC11C in mouse lymphoid tissues (e.g., spleen, lymph nodes) .
Immunohistochemistry: Localizes SEC11A/C in human tonsil and cancer tissues .
Functional Studies: Used to validate SEC11 knockdown/knockout models in studies of ER stress and vesicle trafficking .