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Stress-associated endoplasmic reticulum protein family member 2 (SERP2) is an endoplasmic reticulum (ER) membrane-associated protein that interacts with nascent target proteins during their translocation into the ER lumen and helps protect unfolded proteins from degradation during ER stress. It may facilitate glycosylation of target proteins after ER stress termination and modulate N-glycosylation sites. SERP2 is predicted to have a role in the unfolded protein response, and it is detected in multiple tissues. Its dysfunction or altered expression may contribute to hematologic cancer, and it may be involved in broader cellular stress response pathways[3][4][6][9].
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