LMBR1L antibodies are polyclonal or monoclonal reagents that bind specifically to the LMBR1L protein, a 489-amino-acid transmembrane protein with nine helices. These antibodies enable detection and functional studies of LMBR1L in human, mouse, and rat samples, particularly in immune cells and lymphoid tissues .
LMBR1L antibodies are used to investigate:
Wnt/β-catenin signaling regulation: LMBR1L forms a complex with GP78 and UBAC2 in the endoplasmic reticulum (ER) to degrade Wnt receptors (FZD6, LRP6) and stabilize β-catenin destruction complex components (Axin1, GSK-3α/β) .
Lymphocyte development: Knockout mice lacking LMBR1L exhibit impaired T cell, B cell, and NK cell differentiation, reduced antiviral responses, and increased apoptosis in activated T cells .
Mechanistic studies: Antibodies enable detection of LMBR1L interaction partners (e.g., GP78) and downstream signaling molecules (e.g., β-catenin, TCF-1) via co-immunoprecipitation or Western blot .
LMBR1L deficiency disrupts ER-associated degradation (ERAD) of Wnt receptors, leading to β-catenin accumulation and apoptosis in lymphocytes .
Constitutive phosphorylation of Akt and MAPK pathways occurs in LMBR1L-deficient T cells, indicating dysregulated survival signaling .
Western blot: Detects LMBR1L at ~55–58 kDa in human HepG2 cells and mouse lymphoid tissues .
Immunohistochemistry: Localizes LMBR1L to ER membranes in lymphocyte progenitors .
ELISA: Quantifies LMBR1L expression in serum or lysates, with cross-reactivity confirmed across species .