SERP1
SERP1, the stress-associated endoplasmic reticulum protein 1 (also known as RAMP4), is a small endoplasmic reticulum membrane protein of the RAMP4 family. It interacts with proteins as they are translocated into the ER lumen and helps protect them during ER stress. Browse Assay Genie's current range of SERP1 research reagents below, or read on for the biology behind the target.
SERP1 acts at the point where newly made proteins enter the endoplasmic reticulum. According to UniProt, it interacts with target proteins during their translocation into the lumen of the ER and protects unfolded target proteins against degradation during ER stress. It may also facilitate glycosylation of target proteins after ER stress has ended, and may modulate the use of N-glycosylation sites on those proteins.
The SERP1 gene encodes stress-associated endoplasmic reticulum protein 1, a membrane protein located in the endoplasmic reticulum membrane. HGNC places it in the Sec61 complex subunits gene group, and UniProt classifies it in the RAMP4 family. The human gene has mouse and rat orthologs, both named Serp1, which allows the protein's role in ER protein handling to be studied in common model systems.
The NCBI Gene summary describes SERP1 as predicted to be involved in the endoplasmic reticulum unfolded protein response. It is also predicted to act upstream of or within positive regulation of organ growth, positive regulation of peptide hormone secretion and positive regulation of translation, and it is reported to be located in cytoplasmic microtubule. The name RAMP4 is a commonly used alias, and FLJ43424 is another listed alias. Despite the similar symbol, SERP1 is not a member of the serpin family of protease inhibitors.
SERP1 protects unfolded target proteins from degradation during ER stress, making it relevant to studies of how cells cope with protein-folding load.
It interacts with proteins during translocation into the ER lumen and belongs to the Sec61 complex subunits gene group.
SERP1 may facilitate glycosylation after ER stress and may modulate the use of N-glycosylation sites on target proteins.
SERP1 is predicted to be involved in the ER unfolded protein response, and to act in translation and peptide hormone secretion.
SERP1 interacts with target proteins as they are translocated into the endoplasmic reticulum lumen. It protects unfolded proteins from degradation during ER stress, and it may facilitate their glycosylation once stress has ended. It may also modulate which N-glycosylation sites are used.
The HGNC name is stress associated endoplasmic reticulum protein 1, and UniProt uses Stress-associated endoplasmic reticulum protein 1. Listed aliases are RAMP4 and FLJ43424. Despite the name, SERP1 is a RAMP4 family protein and is unrelated to the SERPIN protease inhibitor genes.
Yes. Both mouse and rat have an ortholog named Serp1, so the protein's role in ER protein handling can be studied in rodent models. Check the datasheet of any product for its validated reactivity.
Serpin-family targets with similar-looking symbols, listed to help you find the right protein; SERP1 itself is an ER membrane protein, not a serpin.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9Y6X1; product specifications from Assay Genie datasheets.