Technical Data
Lysyl Oxidase (LOX, Protein-lysine 6-oxidase)
Protein-lysine-6 oxidase; LOX (EC, a 30kD copper-containing amine oxidase, belongs to a heterogeneous family of enzymes that oxidize primary amine substrates to reactive aldehydes. It plays a vital role in the formation and repair of ECM. Localized both in the cytosol and nucleus, it catalyzes the oxidation and deamination of epsilon-NH2 group of lysine and hydroxylysine residues to alpha-aminoadipic-delta-semialdehyde. This is the first step that initiates the covalent cross-linking of collagen and tropoelastin resulting in the formation of insoluble collagen and elastic fibers in the extracellular matrix. LOX is a multifunctional enzyme having diverse biological functions such as developmental regulation, tumor suppression, cell motility and cellular senescence. Deficiency of LOX is seen in certain carcinomas and 3X-linked recessive human connective tissue disorders—Cutis Laxa.

Suitable for use in Immunofluorescence/Immunocytochemistry, Western Blot, Immunohistochemistry and Immunoprecipitation. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:500
Immunohistochemistry (FFPE): 1:100
Immunohistochemistry: Frozen sections
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
100ul-20°CBlue IceHumanRabbit
Not Determined
Synthetic peptide corresponding to aa305-320 DLLDANTQRRVAEGHK of human LOX. Species Sequence Homology: mouse, chimpanzee; 100%, rat, canine, porcine, bovine; 93%, Xenopus; 81%, chicken, 75%
Supplied as a liquid, 0.025% sodium azide, 50% glycerol.
Recognizes human LOX.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Mariani, T.J., Trackman, P.C., Kagan, H.M., et al., Matrix 12(3), 242-248 (1992). 2. Kaneda, A., Wakazono, K., Tsukamoto, T., et al., Cancer Res. 64 (18), 6410-6415 (2004). 3. Hong, H.H., Pischon, N., Santana, R.B., et al., J. Cell. Physiol. 200(1), 53-62 (2004). 4. Fogelgren, B., Polgar, N., Szauter, K.M., et al., J. Biol. Chem. 280(26), 24690-24697 (2005).