nSMase2 (C-terminal region) polyclonal, anti-human, mouse, rat

Background:
Cellular stress leads to hydrolysis of sphingomyelin to generate lipid second messenger molecules including ceramide, sphingosine, and sphingosine-1-phosphate. A variety of sphingomyelinase activities have been described that differ in tissue and subcellular distribution, as well as pH and cation dependance. These enzymes generate ceramide for specific signaling pathways that lead to a wide range of cellular responses, such as apoptosis, cell cycle arrest, cell survival, and cell proliferation. Neutral sphingomyelinases (nSMases) are Mg2+-dependent neutral pH SMases, and the family includes nSMase1, nSMase2, and nSMase3. These nSMases differ in their tissue distribution and subcellular localization. nSMase2 (also known as SMPD3) is expressed primarily in brain, and co-localizes with Golgi markers in several cell lines. The activity and phosphorylation of nSMase2 is upregulated in response to oxidative stress. In addition, nSMase2 binds calcineurin, and this interaction inhibits nSMase2 activity.

Immunogen: nSMase2 synthetic peptide corresponds to amino acids in the C-terminal region of human nSMase2. This sequence is highly conserved in rat and mouse nSMase2, and has low homology to other nSMase family members.

Specificity: The antibody detects a 78 kDa* band corresponding to nSMase2 on SDS-PAGE immunoblots of adult mouse brain and rat PC12 cells.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.