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Monoclonal Antibody Western Blotting Olfm4

Also showing Monoclonal Antibody Immunohistochemistry Paraffin Olfm4

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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 [1]). 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).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, 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 [1]). 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).