Latexin Proteins, Antibodies, cDNA Clones Research Reagents

LXN (Latexin, also known as ECI; TCI), located on 3q25.32, is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, rat, chicken, zebrafish, and frog. The gene produces a 25750 Da protein composed of 222 amino acids. TLXN is a specific inhibitor of zinc-dependent metallocarboxypeptidases. The protein is an elongated molecule with N- and C-terminal domains that each consist of an alpha helix enveloped by a curved beta-sheet. Diseases such as Endocervicitis and Postsurgical Hypothyroidism are associated with LXN.

Latexin Protein (3)

    Latexin Antibody (13)

      Latexin cDNA Clone (30)

      Latexin Lysate (1)

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        Latexin Background

        Latexin, also known as endogenous carboxypeptidase inhibitor, tissue carboxypeptidase inhibitor, TCI, ECI, and LXN, is a cytoplasm protein that belongs to the protease inhibitor I47 (latexin) family. It is highly expressed in the heart, prostate, ovary, kidney, pancreas, and colon. Latexin / LXN is the only known endogenous specific inhibitor of zinc-dependent metallocarboxypeptidases (MCPs) present in mammalians so far. Latexin is originally identified as a molecular marker for the regional specification of the neocortex in development in rats. The 222 amino acid latexin in the human shows different expression distribution with high levels in heart, prostate, ovary, kidney, pancreas, and colon, but only moderate or low levels in other tissues including the brain. Latexin is also expressed at high levels and is inducible in macrophages in concert with other protease inhibitors and potential protease targets, and thus is suggested to play a role in inflammation and innate immunity pathways. Despite the non-detectable sequence similarity with plant and parasite inhibitors, Latexin is related to a human putative tumor suppressor protein, TIG1. Also, Latexin is implicated in Alzheimer's disease.

        Latexin References

        • Liu Q., et al.,(2000), Cloning, tissue expression pattern and genomic organization of latexin, a human homologue of rat carboxypeptidase A inhibitor. Mol. Biol. Rep. 27:241-246.
        • Gauci S., et al., (2009), Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.nal. Chem. 81:4493-4501.
        • Muzny D.M., et al.,(2006), The DNA sequence, annotation and analysis of human chromosome 3.Nature 440:1194-1198.

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