Elastic fibers provide tissues with elasticity which is critical to the function of arteries, lungs, skin, and other dynamic organs. Loss of elasticity is a major contributing factor in aging and diseases. However, the mechanism of elastic fiber development and assembly is poorly understood. Lysyl oxidases are extracellular copper-dependent enzymes that catalyzing the formation of lysine and hydroxylysine-derived cross-links in collagens and lysine-derived cross-links in elastin. These cross-links are essential for the tensile strength of collagens and the rubber-like properties of elastin, both abundant extracellular matrix proteins that are necessary for the structural integrity and function of connective tissues. Lysyl oxidases (LOX) are involved in cross linking of elastin and collagens and the LOX family comprise of LOX and 4 LOX-like enzymes, all are likely to catalyze cross-linked formation in collagens and elastin. The specific functions associated with these isoforms are not completely understood at present. The LOX are essential and crucial for development of the cardiovascular system and LOX null mice died prenatally of aortic aneurysms and cardiovascular dysfunction (1). LOX family members are also essential for respiratory system and the integrity of elastic and collagen fibers in the lungs and skin.
Lysyl oxidase catalyzes the reaction that generates peptidyl-δ -hydroxy-α -aminoadipic-δ -semialdehyde and peptidyl-α -aminoadipic-δ -semialdehyde from hydroxylysine and lysine residues which is the final enzymatic reaction required for collagen cross linking. The newly formed aldehyldes fromed by these enzymatic reaction then spontaneously react with other aldehydes, unmodified lysine and hydroxylysine to form a variety fo intra and inter molecular cross links that are found in collagens and elastins (2). Lysyl oxidase is a copper-dependent amine oxidase. It is secreted from fibrogenic cells as a pro-enzyme that appears to have little or no enzyme activity, and is processed in the extracellular environment to produce the active 32 kDa enzyme and an 18 kDa propeptide (3). LOXL1 is a 608aa (605in mouse and 400 in human) protein. Antibodies raised against LOXL1 strongly reacted with a 90kDa protein and a 34 kDa smaller subunit essentially the active LOX subunit in PC-LOXL1 samples. The 400 amino acid sequence in human is processed by cleavage of 207 amino acids form the N-terminal.
FabGennix has made rabbit anti-lysyl oxidase like 1 (LOXL1) antibodies using peptide taken from near the carboxy-terminal end of the protein. The LOXL1-selective antibodies were generated against synthetic peptides form unique regions of the LOXL1 protein. The antigenic peptide was post-synthetically covalently modified to achieve the desired antigenicity before using it as immunogen to immunize rabbits. The rabbit antibodies obtained were isolated and purified on an immobilized antigen based affinity matrix before stabilizing them in antibody stabilization buffer. The antibodies to LOXL1 label LOXL1full length and active subunit as 91kDa and 32 kDa bands in PC-LOXL1 smaples. FabGennix Inc. provides Western blot positive controls for LOXL1 in ready-to-use buffer for SDS-PAGE and western blotting applications. Limited quantities of antigenic blocking peptides for this antibody are also available (Inquire before placing orders). For a complete listing of all cycle cycle and mitosis related antibodies, visit our website at www.FabGennix.com.
For research use only, not for diagnostic or therapeutic use.
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