Sortolin-Related Receptor Precursor containing LDLR A repeats (SORLA) Antibodies from MyBioSource.com

Anti-SORLA Antibodies (SORLA-101AP) Alternate Nomenclature: LDLR relative with 11 binding domain repeat, Sorting protein related receptor (SorL/LR11) Sorting protein-related receptor (SORLA/LR11) is a highly conserved mosaic receptor that is expressed by cells in carious tissues including cell of the collecting ducts in the kidney and in neurons of the CNS and peripheral nervous system. The functional features on SORLA/LR11receptor indicate it serves as a sorting receptor shuttling the plasma membrane, endosomes and the Golgi. The terminal oligo saccharides on the SORLA receptors that are synthesized in kidney and brains are modified with terminal beta 1,4 linked GalNAc-4-SO (1). The SORLA receptor interacts with LDL receptor, a protein of approximately 250kDa called LR11 which contained a cluster of 11 LDL receptor binding repeats, a group of 5 LDL receptor YWTD repeats, a learge hexa repeats of elements found in neuronal cell adhesion molecule and a portion similar to yeast receptor for vacuolar protein sorting called VSP10. The oligo saccharides located on the VSP10doamin are modified with beta 1, 4-linked GalNAc when the VPs10 is expressed in cells along with either of two recently coned protein-specific beta 1- 4GalNAc-transferase, galNAcTIII and GalNAcTIV. These highly specific modification on LR11 and VSP10 domains are responsible for SORLA interaction for protein sorting and influence the protein trafficking in cells (1). SORLA protein in neuronal cells is also identified and recognized as neuronal receptor for amyloid precursor protein (APP) that affect its intracellular transport and processing. The expression of SORLA is decreased in Alzheime's patients and elevated levels in amyloid-beta peptide in SORLA-deficient mice suggest the importance of this protein sorting receptor in neurodegenerative disorders. The SORLA receptor directly interacts with beta-site APP cleaving enzyme (BACE) and APP and inhibit the BACE-APP complex formation and SORLA carboxy tail construct significantly inhibits APP shedding in a (BACE) dependent manner. It is suggested that SORLA acts as a trafficking receptor that prevents BACE-APP interactions and hence BACE cleavage of APP and genetic variants in SORLA may be important risk factors for late-onset Alzheimer's disease (2). In transfected experiments about 10% of full length SORLA receptor is expressed on the cell surface capable of mediating endocytosis. The SORLA receptor is regulated by proteolytic cleavage mediated by protease furin at site (50-RRKR-53), the truncated SORLA receptor was found in the late golgi suggesting its interaction with newly synthesized ligands (3). SORLA is a relatively large protein with 2215amino acids with an approximate molecular weight of 250kDa. MyBioSource has made SORLA-specific antibodies in rabbits using peptide methodology. The SORLA receptor antibodies were made against a near carboxyterminal peptide, the peptide was covalently modified post synthesis to achieve the desired antigenecity before coupling to a carrier protein. The SORLA-selective antibodies were affinity purified against immobilized antigen based affinity chromatography and are represented as pure IgG fractions stabilized in antibody stabilization buffer. The affinity purified antibodies can be conjugated as HRP, alkaline phosphatase conjugates or with fluorophores (FITC, Rhodamine) for IHC, Confocal, WB analyses at a nominal price