Product Name: 5 Lipoxygenase (phospho Ser523) Antibody
Species Reactivity: Human, Rat
Tested Applications: WB
Applications: The antibody has been directly tested for reactivity in Western blots with rat and human tissue. It is anticipated that the antibody will react with non human primates based on the fact that these species have 100% homology with the amino acid sequence used as antigen.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 80
Immunogen: Phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser523 of human 5-lipoxygenase (5-LO).
Host Species: Rabbit
Purification: Affinity Purified
Physical State: Liquid
CAS NO.: 40077-57-4
Product: Aviptadil
Buffer: 100 uL in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per mL BSA and 50% glycerol.
Concentration:
Storage Conditions: 5 Lipoxygenase antibody can be stored at -20˚C and is stable at -20˚C for at least 1 year.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: 5-LO, 5LPG, LOG5, 5-LOX,
Accession NO.: P09917
Protein Ino: 126407
Official Symbol: ALOX5
Geneid: 240
Background: The enzyme 5-lipoxygenase (5-LO) plays a key role in regulating the production of leukotrienes (LTs) (Funk, 2001). Overproduction of LTs contributes to several diseases, most notably chronic inflammatory diseases, including asthma (Drazen et al., 1994), fibrosis (Wilborn et al., 1996) and atherosclerosis (Dwyer et al., 2004). Recent work has demonstrated that the activity of 5-LO is regulated by PKA phosphorylation of serine-523 in 5-LO (Luo et al., 2004). Under normal conditions, this phosphorylation may be important in limiting inflammation. Abnormal signaling through cAMP and PKA, then, could contribute to a variety of diseases, including those characterized by chronic inflammation. The phospho-specific antibody to Ser523 on 5-LO is thus likely to provide a valuable tool for studies of the role of 5-LO regulation in diseases such as asthma, fibrosis and atherosclerosis.
PubMed ID:http://aac.asm.org/content/51/11/3988.abstract
