LCN1 Proteins, Antibodies, cDNA Clones, ELISA Kits Research Reagents

LCN1 (Lipocalin 1, also known as TP; TLC; PMFA; VEGP), located on 9q34.3, is conserved in chimpanzee, Rhesus monkey, dog, cow, and rat. The gene produces a 19250 Da protein composed of 176 amino acids. This gene encodes a member of the lipocalin family of small secretory proteins. Diseases such as Dry Eye Syndrome and Lateral Displacement Of Eye are associated with LCN1. The related pathways of LCN1 include Transport of vitamins, nucleosides, and related molecules and Transport of glucose and other sugars, bile salts and organic acids, metal ions, and amine compounds.

LCN1 Protein (1)

    LCN1 Antibody (4)

      LCN1 ELISA Kit & Match Antibody ELISA Pair Set (1)

      LCN1 cDNA Clone (13)


      LCN1 qPCR Primer (1)

      LCN1 Lysate (1)

        LCN1 Background

        Lipocalin-1, also known as Von Ebner gland protein, VEG protein, Tear Prealbumin, VEGP, Tear lipocalin, and LCN1 is a secreted protein that belongs to the calycin superfamily and Lipocalin family. Human Lipocalin-1 / VEGP was originally described as a major protein of human tear fluid, which was thought to be tear specific. Lipocalin-1 / VEGP is identical to lingual von Ebner's gland protein and is also produced in the prostate, nasal mucosa, and tracheal mucosa. Homologous proteins have been found in the rat, pig, and probably dog and horse. Lipocalin-1 / VEGP is an unusual lipocalin member, because of its high promiscuity for relative insoluble lipids and binding characteristics that differ from other members. Lipocalin-1 / VEGP acts as the principal lipid-binding protein in tear fluid, a more general physiological function has to be proposed due to its wide distribution and properties. Lipocalin-1 / VEGP would be ideally suited for scavenging of lipophilic, potentially harmful substances and thus might act as a general protection factor of epithelia. Lipocalin-1 / LCN1 could play a role in taste reception. It could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Lipocalin-1 / LCN1 can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. It exhibits an extremely wide ligand pocket.

        LCN1 References

        • Lassagne H. et al., 1993, Exp. Eye Res. 56:605-609.
        • Redl,B. et al., 2000, Biochim Biophys Acta  1482 (1-2):241-8.
        • Wojnar P. et al., 2001, J. Biol. Chem. 276:20206-20212.
        • Wojnar P. et al., 2003, J. Biol. Chem. 278:16209-16215.
        • Breustedt D.A. et al., 2005, J. Biol. Chem. 280:484-493.

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