LSR
LSR (lipolysis stimulated lipoprotein receptor, also known as LISCH7 or ILDR3) is an immunoglobulin superfamily membrane protein. It is thought to contribute to clearance of triglyceride-rich lipoprotein from blood and helps maintain epithelial barrier function at tricellular tight junctions. Browse Assay Genie's current range of LSR research reagents below, or read on for the biology behind the target.
LSR has two documented roles. In lipid metabolism, it has a probable role in the clearance of triglyceride-rich lipoprotein from the blood. The protein binds chylomicrons, LDL and VLDL in the presence of free fatty acids, and this binding allows the lipoproteins to be taken up into cells. In epithelia, LSR maintains barrier function by recruiting MARVELD2, also called tricellulin, to tricellular tight junctions, the points where three cells meet.
The LSR protein is found at the cell membrane and in tight junctions. It belongs to the immunoglobulin superfamily and to the LISCH7 family, and HGNC places the LSR gene in the group of immunoglobulin like domain containing genes. Researchers working on junction biology or lipoprotein uptake often study LSR alongside tricellin-associated proteins and lipoprotein receptors. Mouse and rat each have an ortholog named Lsr, which allows the protein to be studied in common rodent models.
NCBI Gene summarises LSR as predicted to be involved in establishment of skin barrier, protein localisation to tricellular tight junctions and tricellular tight junction assembly. It is also predicted to act upstream of or within maintenance of the blood-brain barrier. These annotations place LSR at the interface between barrier biology and lipid handling. Besides LSR, the gene has the aliases LISCH7 and ILDR3, and the name reflects its original description in connection with lipolysis-stimulated lipoprotein binding.
LSR is proposed to bind chylomicrons, LDL and VLDL in the presence of free fatty acids and mediate their cellular uptake.
LSR recruits tricellulin (MARVELD2) to tricellular tight junctions, making it a focus for studies of junction assembly.
LSR maintains epithelial barrier function, and is predicted to contribute to establishment of the skin barrier.
LSR is predicted to act upstream of or within maintenance of the blood-brain barrier.
LSR has a probable role in clearing triglyceride-rich lipoprotein from blood. It binds chylomicrons, LDL and VLDL in the presence of free fatty acids, allowing their uptake into cells. It also maintains epithelial barrier function by recruiting tricellulin (MARVELD2) to tricellular tight junctions.
The HGNC full name is lipolysis stimulated lipoprotein receptor. The gene is also known as LISCH7 and ILDR3. The LISCH7 name is also used for the protein family to which LSR belongs, within the immunoglobulin superfamily.
Yes. Both mouse and rat have an ortholog named Lsr, so rodent models can be used to study its roles in lipoprotein handling and barrier function. Check the datasheet of any product for its validated reactivity.
Tight junction proteins, lipoprotein receptors and immunoglobulin-domain family members related to LSR biology.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q86X29; product specifications from Assay Genie datasheets.