High Purity, Bioactive Lysyl Oxidase Homolog 2

Our Bioactive Recombinant Human and Mouse Lysyl Oxidase Homolog 2 offer higher purity than our competitors. Backed by our high quality, consistency between lots, and our reputation for superior customer service, our LOXL2 proteins offer a better value than our competitors’.

  R&D Systems
(Catalog #
Competitor R&D Systems
(Catalog #
Species Human Human Mouse Mouse
Source NS0 CHO NS0 unknown-mammalian
Mass per vial 10 µg 10 µg 10 µg 25 µg     200 µg
>2 >2 >4.5 >3
Purity >90% full length >67% full length >80% full length >19% full length

Our Lysyl Oxidase Homolog 2 Proteins Provide Superior Purity

A. B.

SDS PAGE Highlights Purity. 1 μg/lane of Recombinant Human Lysyl Oxidase Homolog 2 (Catalog # 2639-AO) and 1 μg/lane of competitor Lysyl Oxidase Homolog 2 (A) and 1μg/lane of Recombinant Mouse Lysyl Oxidase Homolog 2 (Catalog # 9259-AO) and 1 μg/lane of competitor Lysyl Oxidase Homolog 2 (B) was resolved with 4-20% SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining.

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Lysyl Oxidase Homolog 2 (lysyl oxidase-like protein 2, LOXL2) is a member of lysyl oxidase-like (LOXL) gene family which includes LOXL1 through LOXL4. These enzymes are secreted copper-binding amine oxidases that oxidize primary amine substrates to aldehydes (1). The N-terminal region of LOXL2 contains four scavenger receptor cysteine-rich (SRCR) domains, and the C-terminal region is a catalytic domain similar to other lysyl oxidases (1). The catalytic domain contains conserved residues required for copper binding and formation of a lysyl tyrosylquinone co-factor (2). It has been shown that LOXL2 promotes cell migration and tumor cell invasiveness (3, 4). Elevated expression of LOXL2 is also associated with cancer progression in various tumors and carcinoma cell lines, which makes it a potential marker for prognosis of cancer (5). LOXL2 is expressed in many tissues, with elevated levels in reproductive tissues such as placenta, uterus, and prostate (6).


  1. Csiszar, H. (2001) Prog. Nucleic Acid Res. Mol. Biol. 70:1.
  2. Maki, J.M. and K.I. Kivirikko (2001) Biochem J. 355:381.
  3. Akiri, G. et al. (2003) Cancer Res. 63:1657.
  4. Hollosi, P. et al. (2009) Int. J. Cancer. 125:318.
  5. Peinado, H. et al. (2008) Cancer Res. 68:4541.
  6. Jourdan-Le Saux C. et al. (1999) J. Biol. Chem. 274:12939.