Human Lysyl Oxidase Homolog 2/LOXL2 Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Data Examples

Western Blot View Larger

Detection of Human Lysyl Oxidase Homolog 2/LOXL2 by Western Blot. Western blot shows lysates of HEC‑1‑B human endometrial adenocarcinoma cell line and U‑87 MG human glioblastoma/astrocytoma cell line. PVDF Membrane was probed with 1 µg/mL of Goat Anti-Human Lysyl Oxidase Homolog 2/LOXL2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2639) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Lysyl Oxidase Homolog 2/LOXL2 at approximately 105 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.

Simple Western View Larger

Detection of Human Lysyl Oxidase Homolog 2/LOXL2 by Simple Western^TM. Simple Western lane view shows lysates of
U‑87 MG human glioblastoma/astrocytoma cell line, loaded at 0.2 mg/mL. A specific band was detected for Lysyl Oxidase Homolog 2/LOXL2 at approximately 109 kDa (as indicated) using 10 µg/mL of Goat Anti-Human Lysyl Oxidase Homolog 2/LOXL2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2639) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the
12-230 kDa separation system.

Preparation and Storage

Background: Lysyl Oxidase Homolog 2/LOXL2

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). Although some of the LOXL enzymes are known to cross-link collagen and elastin substrates, such a function has yet to be characterized for LOXL2. 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).

Product Datasheets

Related Research Areas

• Additional Reduction/Oxidation (Redox) Enzymes
• HIF Transcription Factors
• Oxidases and Oxygenases
• Oxygenases/Hydroxylases
• Redox Enzymes