Application Methods: Immunohistochemistry (Paraffin), Western Blotting
Background: Olfactomedin-4 (OLFM4, hGC-1) is a member of the Olfactomedin family, a small group of extracellular proteins defined by the presence of a conserved "Olfactomedin domain" that is thought to facilitate protein-protein interactions (1). OLFM4 is a secreted glycoprotein, which forms disulfide bond-mediated oligomers, and is thought to mediate cell adhesion through its interactions with extracellular matrix proteins such as lectins (2). Human OLFM4 was first cloned from myeloid cells (3) and is expressed in a distinct subset of neutrophils, though the functional significance of this differential expression pattern remains unclear (4). Among normal tissues, the expression of OLFM4 protein is most abundant in intestinal crypts (5), where it has garnered attention as a possible marker of intestinal stem cells (6). Notably, OLFM4 expression is markedly increased in several tumor types, including colorectal, gastric, pancreas, lung, and breast (reviewed in ). Furthermore, research studies show that the expression levels of OLFM4 vary in relation to the severity and/or differentiation status of multiple tumor types (1, 6-8), leading to the suggestion that OLFM4 may have utility as a prognostic marker in some cancer patients (9).
|Human, Mouse, Rat|
Application Methods: Immunofluorescence (Frozen), Immunoprecipitation, Western Blotting
Background: Chloride channel 3 (CLCN3) is a voltage-gated chloride channel (CIC) family protein that mediates H+/Cl- exchange across cell membranes. This 818 amino acid, multi-pass membrane protein is highly expressed in the brain and is especially abundant in the olfactory bulb, hippocampus, and cerebellum (1). CLCN3 protein localizes to endosomal compartments and synaptic vesicles where it contributes to vesicle acidification and proper synaptic vesicle neurotransmitter loading for GABAergic synaptic transmission (2,3). CAMKII-mediated phosphorylation of CLCN3 regulates chloride channel activity by regulating cell surface targeting of the CLCN3 chloride channel (4). Research studies show abnormally high CLCN3 expression at the cell surface of human glioma cells, and that CAMKII-dependent regulation of these channels contributes to glioma invasion (5).