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ASM Mouse anti-Human, Clone: OTI3H7, Invitrogen™

Mouse Monoclonal Antibody

Manufacturer:  Invitrogen MA526615

Catalog No. PIMA526615


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Description

Description

Human acid sphingomyelinase (sphingomyelin phosphodiesterase, ASM) is the lysosomal enzyme responsible for the hydrolysis of sphingomyelin to ceramide and phosphocholine. Converts sphingomyelin to ceramide. aSM also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerol-phosphoglycerol. The enzyme is a membrane-associated glycoprotein with a pH optimum of about 4.5 and a subunit molecular mass of about 72 kDa. In addition AtoS M, two other sphingomyelinases have been identified in man, a Mg2+- dependent neutral sphingomyelinase found primarily in brain and a Zn2+-dependent acid sphingomyelinase found primarily in serum. Although it is likely that the acid and neutral sphingomyelinases are coded by different genes, the molecular genetic relationship of these three biochemically distinct sphingomyelinases has not been determined. Understanding the role of these sphingomyelinases in the hydrolysis of sphingomyelin to ceramide will be an important step in the understanding of ceramide as it is further hydrolyzed to sphingosine, a neutral phospholipid which has been implicated in the regulation of protein kinase C-mediated signal transduction. Inherited deficiencies of ASM have been reported in man, deficient ASM activity results in the two major subtypes of Niemann-Pick disease (NPD).
Specifications

Specifications

ASM
Monoclonal
1 mg/mL
PBS with 1% BSA, 50% glycerol and 0.02% sodium azide; pH 7.3
P17405
Sphingomyelin phosphodiesterase (EC:3.1.4.12); Acid sphingomyelinase; aSMase; SMPD1; ASM
Mouse
IgG1
100 μL
-20° C, Avoid Freeze/Thaw Cycles
Primary
6609
Immunohistochemistry (Paraffin), Western Blot
OTI3H7
Unconjugated
SMPD1
Liquid
SMPD1
Human recombit protein fragment corresponding to amino acids 62-341 of SMPD1 produced in E.coli
Affinity Chromatography
RUO
Antibody
Monoclonal
Human
Documents
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