OLFML1 antibodies target the OLFML1 protein (UniProt ID: Q6UWY5), a 402-amino acid glycoprotein containing three N-glycosylation sites (residues 66, 138, 183) . This protein belongs to the olfactomedin domain-containing family and enhances cell cycle progression in cancer cell lines by increasing the percentage of S-phase cells . Its observed molecular weight (60 kDa) exceeds the calculated 46 kDa due to glycosylation .
OLFML1 promotes cell proliferation in human cancer cell lines (e.g., Caco-2, U-251, HuH-7) via S-phase acceleration . Its secretion and glycosylation are critical for this function, as shown in vitro studies .
OLFML1 interacts with the Nogo A receptor (NgR1) complex, modulating axonal growth. Key findings include:
NgR1 Binding: OLFML1 binds NgR1, disrupting its interaction with coreceptors p75NTR and LINGO-1, thereby attenuating growth cone collapse in dorsal root ganglia neurons .
Neuronal Localization: Colocalizes with NgR1 in retinal ganglion cells and DRG neurons, suggesting roles in neurite development .
Interaction Partner | Functional Impact | Study Model |
---|---|---|
NgR1 | Inhibits myelin-induced axon growth suppression | Mouse DRG neurons |
β-dystrobrevin | Cytoskeletal scaffolding | PC12 cells |
WAVE1 | Apoptosis regulation | Ischemic mouse cortex |
Western Blot: Detected in Caco-2, U-251, and HuH-7 cell lysates, as well as mouse/rat liver and testis tissues .
Biolayer Interferometry: Proteintech’s 84454-1-RR shows high affinity (0.807 nM) for human OLFML1 .
Immunohistochemistry: Strong reactivity in human small intestine, liver, and retinal tissues .
Cross-Reactivity: No cross-reactivity with OLFML2 or OLFML3 reported .
Glycosylation Effects: Antibodies detect glycosylated forms, explaining higher observed vs. calculated molecular weights .
OLFML1 antibodies are pivotal in studying:
Cancer cell proliferation mechanisms.
Axon regeneration pathways in neurological disorders.
Protein interaction networks involving NgR1 and Wnt signaling modulators.